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Information on EC 2.7.7.65 - diguanylate cyclase
for references in articles please use BRENDA:EC2.7.7.65
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EC Tree 2 Transferases
2.7 Transferring phosphorus-containing groups
2.7.7 Nucleotidyltransferases
2.7.7.65 diguanylate cyclase
IUBMB Comments
A GGDEF-domain-containing protein that requires Mg2+ or Mn2+ for activity. The enzyme can be activated by BeF3, a phosphoryl mimic, which results in dimerization . Dimerization is required but is not sufficient for diguanylate-cyclase activity . Cyclic di-3′,5′-guanylate is an intracellular signalling molecule that controls motility and adhesion in bacterial cells. It was first identified as having a positive allosteric effect on EC 2.4.1.12, cellulose synthase (UDP-forming) .
The enzyme appears in viruses and cellular organisms
- 2.7.7.65
- phosphodiesterase
- cyclases
- aeruginosa
- monophosphate
- cyclic-di-gmp
- exopolysaccharide
-
flagellar
-
plankton
-
sessile
-
c-di-gmp-dependent
-
swarming
- caulobacter
- hd-gyp
-
i-site
- crescentus
-
diguanosine
-
c-di-gmp-mediated
-
per-arnt-sim
-
cyanobacteriochromes
- xylinum
-
ggdef-eal
- medicine
- molecular biology
- synthesis
- biotechnology
showSynonyms
diguanylate cyclase, tlr0924, pa3177, vc0395_0300, all2874, pa0847, slr1143, ggdef domain-containing protein, xac0610, pgn_1932, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AdrA
ALL2874
BP3507
Bpe-GReg
cAMP-dependent diguanylate cyclase
-
CdgA
CdgH
cdgJ
cGMP-specific phosphodiesterase
UniProt
Chp8
Dcsbis
DGC
Dgc1
DgcA
DgcP
diguanylate cyclase
diguanylate kinase
DosC
DosD
GcbA
gcbC
GCDC
GcpA
GcsA
GGDEF domain-containing protein
GGDEF family protein
globin-coupled diguanylate cyclase
heme-based globin-coupled diguanylate cyclase
HsbD
ML1419
PA0847
PA2771
PA3177
Pfl01_4666
PGN_1932
PleD
PP_3711
sadC
TM_1788
VC0395_0300
VCA0965
VC_1067
VC_A0965
WspR
XOO3988
YddV
YdeH
YfiN
cdgJ
Vibrio cholerae serotype O1 A1552
-
-
-
DGC
Vibrio cholerae serotype O1 A1552
-
-
-
PleD
response regulator with diguanylate cyclase (GGDEF) domain, Rec domain (D1) and Rec-like adaptor domain (D2)
VCA0965
Vibrio cholerae serotype O1 C6706str2
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 GTP = 2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
cyclization
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SYSTEMATIC NAME
IUBMB Comments
GTP:GTP guanylyltransferase
A GGDEF-domain-containing protein that requires Mg2+ or Mn2+ for activity. The enzyme can be activated by BeF3, a phosphoryl mimic, which results in dimerization [3]. Dimerization is required but is not sufficient for diguanylate-cyclase activity [3]. Cyclic di-3',5'-guanylate is an intracellular signalling molecule that controls motility and adhesion in bacterial cells. It was first identified as having a positive allosteric effect on EC 2.4.1.12, cellulose synthase (UDP-forming) [1].
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CAS REGISTRY NUMBER
COMMENTARY
146316-82-7
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
GTP + GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
GTP + GTP
cyclic-di-3',5'-GMP + diphosphate + diphosphate
Substrates: pH 7.8
Products: reaction stop with 25 mM EDTA, pH 6, KD (cyclic-di-3,5-GMP): 0.3 microM or 0.4 microM (in presence of activator BeF3)
Products: reaction stop with 25 mM EDTA, pH 6, KD (cyclic-di-3,5-GMP): 0.3 microM or 0.4 microM (in presence of activator BeF3)
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: the enzyme uses its GGDEF domain for catalysis. The DgcP of Caulobacter crescentus binds dimeric c-di-GMP at an allosteric site I-site that is characterized by the RxxD motif. Binding of cyclic-di-GMP at the I-site accounts for a strong non-competitive product inhibition, which establishes a limit on the cellular c-di-GMP concentration
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: the enzyme uses its GGDEF domain for catalysis. The DgcP of Caulobacter crescentus binds dimeric c-di-GMP at an allosteric site I-site that is characterized by the RxxD motif. Binding of cyclic-di-GMP at the I-site accounts for a strong non-competitive product inhibition, which establishes a limit on the cellular c-di-GMP concentration
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
A0A170Y3L9
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
A0A170Y3L9
Substrates: the enzyme uses its GGDEF domain for catalysis. The GGDEF signature domain forms part of the active site A-site where GTP is bound (one molecule of GTP substrate per monomer)
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: the enzyme uses its GGDEF domain for catalysis. The GGDEF signature domain forms part of the active site A-site where GTP is bound (one molecule of GTP substrate per monomer)
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: the enzyme uses its GGDEF domain for catalysis. The GGDEF signature domain forms part of the active site A-site where GTP is bound (one molecule of GTP substrate per monomer)
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: the enzyme uses its GGDEF domain for catalysis. The GGDEF signature domain forms part of the active site A-site where GTP is bound (one molecule of GTP substrate per monomer)
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: the enzyme uses its GGDEF domain for catalysis. The GGDEF signature domain forms part of the active site A-site where GTP is bound (one molecule of GTP substrate per monomer)
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: the enzyme uses its GGDEF domain for catalysis. The GGDEF signature domain forms part of the active site A-site where GTP is bound (one molecule of GTP substrate per monomer)
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: the enzyme uses its GGDEF domain for catalysis. The GGDEF signature domain forms part of the active site A-site where GTP is bound (one molecule of GTP substrate per monomer)
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: the enzyme uses its GGDEF domain for catalysis. The GGDEF signature domain forms part of the active site A-site where GTP is bound (one molecule of GTP substrate per monomer)
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: the enzyme uses its GGDEF domain for catalysis. The GGDEF signature domain forms part of the active site A-site where GTP is bound (one molecule of GTP substrate per monomer)
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: the enzyme uses its GGDEF domain for catalysis. The GGDEF signature domain forms part of the active site A-site where GTP is bound (one molecule of GTP substrate per monomer)
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Pseudomonas fluorescens Pfl01
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: the enzyme uses its GGDEF domain for catalysis. The GGDEF signature domain forms part of the active site A-site where GTP is bound (one molecule of GTP substrate per monomer)
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: the enzyme uses its GGDEF domain for catalysis. The GGDEF signature domain forms part of the active site A-site where GTP is bound (one molecule of GTP substrate per monomer)
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: the enzyme uses its GGDEF domain for catalysis. The GGDEF signature domain forms part of the active site A-site where GTP is bound (one molecule of GTP substrate per monomer)
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: the enzyme uses its GGDEF domain for catalysis. The GGDEF signature domain forms part of the active site A-site where GTP is bound (one molecule of GTP substrate per monomer)
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: conversion is enhanced under blue light irradiation, with 38fold difference between the blue and green light-induced activities
Products: conversion is enhanced under blue light irradiation, with 38fold difference between the blue and green light-induced activities
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: the enzyme uses its GGDEF domain for catalysis. The GGDEF signature domain forms part of the active site A-site where GTP is bound (one molecule of GTP substrate per monomer)
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Vibrio cholerae serotype O1 A1552
-
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: the enzyme uses its GGDEF domain for catalysis. The GGDEF signature domain forms part of the active site A-site where GTP is bound (one molecule of GTP substrate per monomer)
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: the enzyme uses its GGDEF domain for catalysis. The GGDEF signature domain forms part of the active site A-site where GTP is bound (one molecule of GTP substrate per monomer)
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Q8PPS5
Substrates: -
Products: -
Products: -
?
GTP
cyclic di-3',5'-guanylate + diphosphate
-
Substrates: -
Products: -
Products: -
?
GTP
cyclic di-3',5'-guanylate + diphosphate
-
Substrates: -
Products: -
Products: -
?
GTP
cyclic di-3',5'-guanylate + diphosphate
-
Substrates: diguanylate cyclase activity constitutes the signaling output of the PleD response regulator
Products: -
Products: -
?
GTP
cyclic di-3',5'-guanylate + diphosphate
Substrates: -
Products: -
Products: -
?
GTP
cyclic di-3',5'-guanylate + diphosphate
Substrates: -
Products: -
Products: -
?
GTP
cyclic di-3',5'-guanylate + diphosphate
-
Substrates: -
Products: -
Products: -
?
GTP
cyclic di-3',5'-guanylate + diphosphate
-
Substrates: -
Products: -
Products: -
?
GTP
cyclic di-3',5'-guanylate + diphosphate
Cereibacter sphaeroides RSP3513
-
Substrates: -
Products: -
Products: -
?
GTP
cyclic di-3',5'-guanylate + diphosphate
-
Substrates: -
Products: -
Products: -
?
GTP
cyclic di-3',5'-guanylate + diphosphate
-
Substrates: -
Products: -
Products: -
?
GTP
cyclic di-3',5'-guanylate + diphosphate
Substrates: -
Products: -
Products: -
?
GTP
cyclic di-3',5'-guanylate + diphosphate
Substrates: -
Products: -
Products: -
?
GTP
cyclic di-3',5'-guanylate + diphosphate
-
Substrates: -
Products: -
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?
GTP
cyclic di-3',5'-guanylate + diphosphate
Substrates: -
Products: -
Products: -
?
GTP
cyclic di-3',5'-guanylate + diphosphate
-
Substrates: -
Products: -
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GTP
cyclic di-3',5'-guanylate + diphosphate
-
Substrates: SwDGC has both cyclase and phosphodiesterase activities. Peaks for c-di-GMP and pGpG (5'-phosphoguanylyl-(3',5')-guanosine) appear within several min of reaction
Products: -
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?
GTP
cyclic di-3',5'-guanylate + diphosphate
-
Substrates: -
Products: -
Products: -
?
GTP
cyclic di-3',5'-guanylate + diphosphate
-
Substrates: -
Products: -
Products: -
?
GTP
cyclic di-3',5'-guanylate + diphosphate
Substrates: -
Products: -
Products: -
?
GTP
diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
GTP
diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
GTP
diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
GTP
diphosphate + cyclic di-3',5'-guanylate
-
Substrates: -
Products: -
Products: -
?
GTP
diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
GTP + GTP
cyclic di-3',5'-guanylate + diphosphate + diphosphate
-
Substrates: pH 8, 60 min, 25°C, 10 mM MgCl2
Products: reaction stop by 0.083 mM EDTA
Products: reaction stop by 0.083 mM EDTA
?
GTP + GTP
cyclic di-3',5'-guanylate + diphosphate + diphosphate
Substrates: -
Products: analyses by pyrophosphatase-coupled spectrophotometric assay
Products: analyses by pyrophosphatase-coupled spectrophotometric assay
?
GTP + GTP
cyclic di-3',5'-guanylate + diphosphate + diphosphate
-
Substrates: 2 mM Mg2+
Products: analysis by coupled spectrophotometric assay measuring diphosphate synthesis or by reverse-phase HPLC
Products: analysis by coupled spectrophotometric assay measuring diphosphate synthesis or by reverse-phase HPLC
?
GTP + GTP
cyclic di-3',5'-guanylate + diphosphate + diphosphate
-
Substrates: 2 mM Mg2+, 25°C
Products: analysis by coupled spectrophotometric assay measuring diphosphate synthesis or by reverse-phase HPLC
Products: analysis by coupled spectrophotometric assay measuring diphosphate synthesis or by reverse-phase HPLC
?
GTP + GTP
cyclic di-3',5'-guanylate + diphosphate + diphosphate
-
Substrates: 2 mM Mg2+, 25°C
Products: analysis by coupled spectrophotometric assay measuring diphosphate synthesis or by reverse-phase HPLC
Products: analysis by coupled spectrophotometric assay measuring diphosphate synthesis or by reverse-phase HPLC
?
GTP + GTP
cyclic di-3',5'-guanylate + diphosphate + diphosphate
-
Substrates: 2 mM Mg2+, 25°C
Products: analysis by coupled spectrophotometric assay measuring diphosphate synthesis or by reverse-phase HPLC
Products: analysis by coupled spectrophotometric assay measuring diphosphate synthesis or by reverse-phase HPLC
?
GTP + GTP
cyclic di-3',5'-guanylate + diphosphate + diphosphate
-
Substrates: 2 mM Mg2+, 25°C
Products: analysis by coupled spectrophotometric assay measuring diphosphate synthesis or by reverse-phase HPLC
Products: analysis by coupled spectrophotometric assay measuring diphosphate synthesis or by reverse-phase HPLC
?
GTP + GTP
cyclic di-3',5'-guanylate + diphosphate + diphosphate
-
Substrates: 2 mM Mg2+, 25°C
Products: analysis by coupled spectrophotometric assay measuring diphosphate synthesis or by reverse-phase HPLC
Products: analysis by coupled spectrophotometric assay measuring diphosphate synthesis or by reverse-phase HPLC
?
GTP + GTP
cyclic di-3',5'-guanylate + diphosphate + diphosphate
-
Substrates: 2 mM Mg2+, 25°C
Products: analysis by coupled spectrophotometric assay measuring diphosphate synthesis or by reverse-phase HPLC
Products: analysis by coupled spectrophotometric assay measuring diphosphate synthesis or by reverse-phase HPLC
?
additional information
?
-
-
Substrates: MifA and MifB proteins act posttranscriptionally on flagellation
Products: -
Products: -
?
additional information
?
-
-
Substrates: analysis of the DGC specificity, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: on-rates constants of substrate and product range between 100/sec and 300/sec
Products: -
Products: -
?
additional information
?
-
Substrates: on-rates constants of substrate and product range between 100/sec and 300/sec
Products: -
Products: -
?
additional information
?
-
-
Substrates: mode of GTPalphaS/Mg2+-binding suggests two-metal catalytic mechanism analogous to adenylate cyclases
Products: -
Products: -
?
additional information
?
-
Substrates: mode of GTPalphaS/Mg2+-binding suggests two-metal catalytic mechanism analogous to adenylate cyclases
Products: -
Products: -
?
additional information
?
-
-
Substrates: analysis of the DGC specificity, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: no substrate: ATP, ADP, AMP, GDP, GMP,CTP, TTP, c-di-GMP, cAMP, and cGMP
Products: -
Products: -
?
additional information
?
-
Cereibacter sphaeroides RSP3513
-
Substrates: no substrate: ATP, ADP, AMP, GDP, GMP,CTP, TTP, c-di-GMP, cAMP, and cGMP
Products: -
Products: -
?
additional information
?
-
-
Substrates: analysis of the DGC specificity, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: cyclic guanylate cyclase YvvD and Dos, a heme based oxygen sensor with cyclic diguanylate phosphodiesterase activity may be part of a fine-tuning mechanism for regulating the intracellular levels of cyclic diguanylate
Products: -
Products: -
?
additional information
?
-
-
Substrates: the interaction between MANT (2'(3'))-O-(N-methylanthraniloyl)- or TNP (2',3'-O-(2,4,6-trinitrophenyl))-substituted nucleotides and the DGC YdeH by fluorimetric and mass-spectrometric means is investigated. A strong fluorescence resonance energy transfer between tryptophan and tyrosine residues of YdeH and the MANT group of MANT-NTPs (MANT-ATP,-CTP, -GTP, -ITP, -UTP, and -XTP) and an enhanced direct MANT fluorescence upon interaction with YdeH is observed
Products: -
Products: -
?
additional information
?
-
Substrates: analysis of the DGC specificity, overview
Products: -
Products: -
?
additional information
?
-
Substrates: analysis of the DGC specificity, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: purified enzyme shows phosphodiesterase activity, but no diguanylate cyclase activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: pppGpG co-purified with reaction products, possible intermediate of diguanylate cyclisation
Products: -
Products: -
?
additional information
?
-
Substrates: HsbD interacts with the anti-anti-sigma factor HsbA, this interaction is lost when the HsbA phosphorylation site, Ser56, is substituted. In contrast, a phosphorylated mimicry of HsbA, engineered by replacing Ser56 with an aspartate residue, interacts more strongly with HsbDs, suggesting that phosphorylation of HsbA possibly strengthens the stability of the HsbDs/HsbA complex with an alanine. HsbD binds to the phosphorylated form of the anti-anti-sigma factor HsbA
Products: -
Products: -
?
additional information
?
-
-
Substrates: HsbD interacts with the anti-anti-sigma factor HsbA, this interaction is lost when the HsbA phosphorylation site, Ser56, is substituted. In contrast, a phosphorylated mimicry of HsbA, engineered by replacing Ser56 with an aspartate residue, interacts more strongly with HsbDs, suggesting that phosphorylation of HsbA possibly strengthens the stability of the HsbDs/HsbA complex with an alanine. HsbD binds to the phosphorylated form of the anti-anti-sigma factor HsbA
Products: -
Products: -
?
additional information
?
-
-
Substrates: analysis of the DGC specificity, overview
Products: -
Products: -
?
additional information
?
-
Substrates: HsbD interacts with the anti-anti-sigma factor HsbA, this interaction is lost when the HsbA phosphorylation site, Ser56, is substituted. In contrast, a phosphorylated mimicry of HsbA, engineered by replacing Ser56 with an aspartate residue, interacts more strongly with HsbDs, suggesting that phosphorylation of HsbA possibly strengthens the stability of the HsbDs/HsbA complex with an alanine. HsbD binds to the phosphorylated form of the anti-anti-sigma factor HsbA
Products: -
Products: -
?
additional information
?
-
Substrates: diguanylate cyclase GcbC physically interacts with the effector protein LapD in order to promote biofilm formation
Products: -
Products: -
?
additional information
?
-
-
Substrates: diguanylate cyclase GcbC physically interacts with the effector protein LapD in order to promote biofilm formation
Products: -
Products: -
?
additional information
?
-
Pseudomonas fluorescens Pfl01
Substrates: diguanylate cyclase GcbC physically interacts with the effector protein LapD in order to promote biofilm formation
Products: -
Products: -
?
additional information
?
-
-
Substrates: GcsA has no PDE activity
Products: -
Products: -
?
additional information
?
-
Substrates: GcsA has no PDE activity
Products: -
Products: -
?
additional information
?
-
Substrates: GcsA has no PDE activity
Products: -
Products: -
?
additional information
?
-
Substrates: GcsA has no PDE activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: GcsA has no PDE activity
Products: -
Products: -
?
additional information
?
-
Substrates: GcsA has no PDE activity
Products: -
Products: -
?
additional information
?
-
Substrates: no substrate: ATP
Products: -
Products: -
?
additional information
?
-
-
Substrates: analysis of the DGC specificity, overview
Products: -
Products: -
?
additional information
?
-
Vibrio cholerae serotype O1 A1552
-
Substrates: analysis of the DGC specificity, overview
Products: -
Products: -
?
additional information
?
-
Q8PPS5
Substrates: sequential random binding model of two identical substrates binding to two equivalent GGDEF domains that come together to form a symmetrical active site
Products: -
Products: -
?
additional information
?
-
-
Substrates: sequential random binding model of two identical substrates binding to two equivalent GGDEF domains that come together to form a symmetrical active site
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
GTP
cyclic di-3',5'-guanylate + diphosphate
-
Substrates: diguanylate cyclase activity constitutes the signaling output of the PleD response regulator
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
A0A170Y3L9
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Pseudomonas fluorescens Pfl01
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Vibrio cholerae serotype O1 A1552
-
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
GTP
diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
GTP
diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
GTP
diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
GTP
diphosphate + cyclic di-3',5'-guanylate
-
Substrates: -
Products: -
Products: -
?
GTP
diphosphate + cyclic di-3',5'-guanylate
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: MifA and MifB proteins act posttranscriptionally on flagellation
Products: -
Products: -
?
additional information
?
-
-
Substrates: cyclic guanylate cyclase YvvD and Dos, a heme based oxygen sensor with cyclic diguanylate phosphodiesterase activity may be part of a fine-tuning mechanism for regulating the intracellular levels of cyclic diguanylate
Products: -
Products: -
?
additional information
?
-
Substrates: HsbD interacts with the anti-anti-sigma factor HsbA, this interaction is lost when the HsbA phosphorylation site, Ser56, is substituted. In contrast, a phosphorylated mimicry of HsbA, engineered by replacing Ser56 with an aspartate residue, interacts more strongly with HsbDs, suggesting that phosphorylation of HsbA possibly strengthens the stability of the HsbDs/HsbA complex with an alanine. HsbD binds to the phosphorylated form of the anti-anti-sigma factor HsbA
Products: -
Products: -
?
additional information
?
-
-
Substrates: HsbD interacts with the anti-anti-sigma factor HsbA, this interaction is lost when the HsbA phosphorylation site, Ser56, is substituted. In contrast, a phosphorylated mimicry of HsbA, engineered by replacing Ser56 with an aspartate residue, interacts more strongly with HsbDs, suggesting that phosphorylation of HsbA possibly strengthens the stability of the HsbDs/HsbA complex with an alanine. HsbD binds to the phosphorylated form of the anti-anti-sigma factor HsbA
Products: -
Products: -
?
additional information
?
-
Substrates: HsbD interacts with the anti-anti-sigma factor HsbA, this interaction is lost when the HsbA phosphorylation site, Ser56, is substituted. In contrast, a phosphorylated mimicry of HsbA, engineered by replacing Ser56 with an aspartate residue, interacts more strongly with HsbDs, suggesting that phosphorylation of HsbA possibly strengthens the stability of the HsbDs/HsbA complex with an alanine. HsbD binds to the phosphorylated form of the anti-anti-sigma factor HsbA
Products: -
Products: -
?
additional information
?
-
Substrates: diguanylate cyclase GcbC physically interacts with the effector protein LapD in order to promote biofilm formation
Products: -
Products: -
?
additional information
?
-
-
Substrates: diguanylate cyclase GcbC physically interacts with the effector protein LapD in order to promote biofilm formation
Products: -
Products: -
?
additional information
?
-
Pseudomonas fluorescens Pfl01
Substrates: diguanylate cyclase GcbC physically interacts with the effector protein LapD in order to promote biofilm formation
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
heme
the most active form of MBP-tagged YddV has an 5-coordinate Fe(III) heme complex. Heme distal residues play key regulatory roles by mediating signal transduction between the sensing and functional domains
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
the most active form of MBP-tagged YddV has an 5-coordinate Fe(III) heme complex
Mg2+
Mn2+
Zn2+
additional information
Mg2+
or Mn2+, strictly required, with Mn2+ resulting in slightly higher activity than Mg2+
Mg2+
required for diguanylate cyclase activity, Kd value 10.5 mM
Mn2+
or Mg2+, strictly required, with Mn2+ resulting in slightly higher activity than Mg2+
Zn2+
enzyme is regulated allosterically by zinc. In vitro, zinc reversibly inhibits DgcZ with a subfemtomolar Ki constant. In vivo, bacterial biofilm formation is modulated by externally applied zinc in a DgcZ- and cyclic di-GMP-dependent fashion
additional information
PleD contains an extra metal binding site or beryllium metal for activation
additional information
-
PleD contains an extra metal binding site or beryllium metal for activation
additional information
catalysis requires either Mg2+ or Mn2+, other divalent metal ions (Ca2+, Co2+, Ni2+, Zn2+, and Cd2+) give no activity
additional information
-
catalysis requires either Mg2+ or Mn2+, other divalent metal ions (Ca2+, Co2+, Ni2+, Zn2+, and Cd2+) give no activity
additional information
in the EcGReg globin domain, the distal residue Tyr43 stabilizes O2 to ferrous ion
additional information
-
in the EcGReg globin domain, the distal residue Tyr43 stabilizes O2 to ferrous ion
additional information
-
poor activating effects by Mg2+, K+, and Na+ at 1-10 mM
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2',3'-O-[4-(dihydroxyiminio)-2,6-dinitrocyclohexa-2,5-diene-1,1-diyl]guanosine 5'-triphosphate
2-(5-amino-1,3,4-thiadiazol-2-yl)-N'-[(1E,2E)-3-(3-nitrophenyl)prop-2-en-1-ylidene]acetohydrazide
4% inhibition at 0.1 mM
3-(3,5-dioxo-2,3,4,5-tetrahydro-1,2,4-triazin-6-yl)-N'-[(E)-(4-nitrophenyl)methylidene]propanehydrazide
11.0% inhibition at 0.1 mM
3-O-alpha-L-rhamnopyranosyl-(1-2)-beta-D-galactopyranosyl-(1-2)-beta-D-glucuronopyranosyl soyasapogenol B 22-O-alpha-D-glucopyranoside
3-O-alpha-L-rhamnopyranosyl-(1->2)-beta-D-galactopyranosyl-(1->2)-beta-D-glucuronopyranosyl soyasapogenol B 22-O-alpha-D-glucopyranoside
3-O-alpha-L-rhamnopyronosyl-(1->2)-beta-D-galactopyranosyl-(1->2)-beta-D-gluconopyranosyl soyasapogenol B 22-o-alpha-D-glucopyranoside
potent non-competitive inhibitor in vitro, not membrane-permeable
9-(3-[4-[(2-amino-6-chloro-9H-purin-9-yl)methyl]-1H-1,2,3-triazol-1-yl]propyl)-6-chloro-9H-purin-2-amine
cyclic 3',5'-diguanylate
-
product inhibition is due to domain immobilization and sets an upper limit for the concentration of this second messenger in the cell
cyclic di-GMP
binding at the inhibitory site mediates dimer formation and inactivation
cyclic-di-3',5'-GMP
allosteric feedback, product inhibition, independent of activation status, binding induces change in conformation and protein-solvent interactions
D-glucuronopyranosyl soyasapogenol B 22-O-alpha-D-glucopyranoside
-
isolated from Pisum sativum, specific and highly potent inhibition of enzyme
N'-((1E)-(4-ethoxy-3-[(8-oxo-1,5,6,8-tetrahydro-2H-1,5-methanopyrido[1,2-a][1,5]diazocin-3(4H)-yl)methylphenyl)methylene)]-3,4,5-trihydroxybenzohydrazide
N'-[(E)-(2,4-dihydroxyphenyl)methylidene]-4-methyl-3-nitrobenzene-1-sulfonohydrazide
17% inhibition at 0.1 mM; 6% inhibition at 0.1 mM
N'-[(E)-(2-hydroxyphenyl)methylidene]-4-methyl-3-nitrobenzene-1-sulfonohydrazide
13% inhibition at 0.1 mM
2',3'-O-[4-(dihydroxyiminio)-2,6-dinitrocyclohexa-2,5-diene-1,1-diyl]guanosine 5'-triphosphate
-
2',3'-O-[4-(dihydroxyiminio)-2,6-dinitrocyclohexa-2,5-diene-1,1-diyl]guanosine 5'-triphosphate
A0A170Y3L9
-
2',3'-O-[4-(dihydroxyiminio)-2,6-dinitrocyclohexa-2,5-diene-1,1-diyl]guanosine 5'-triphosphate
-
2',3'-O-[4-(dihydroxyiminio)-2,6-dinitrocyclohexa-2,5-diene-1,1-diyl]guanosine 5'-triphosphate
-
2',3'-O-[4-(dihydroxyiminio)-2,6-dinitrocyclohexa-2,5-diene-1,1-diyl]guanosine 5'-triphosphate
-
2',3'-O-[4-(dihydroxyiminio)-2,6-dinitrocyclohexa-2,5-diene-1,1-diyl]guanosine 5'-triphosphate
-
2',3'-O-[4-(dihydroxyiminio)-2,6-dinitrocyclohexa-2,5-diene-1,1-diyl]guanosine 5'-triphosphate
-
2'-O-[2-(methylamino)benzoyl]guanosine 5'-(gammaS)triphosphate
-
2'-O-[2-(methylamino)benzoyl]guanosine 5'-(gammaS)triphosphate
A0A170Y3L9
-
2'-O-[2-(methylamino)benzoyl]guanosine 5'-(gammaS)triphosphate
-
2'-O-[2-(methylamino)benzoyl]guanosine 5'-(gammaS)triphosphate
-
2'-O-[2-(methylamino)benzoyl]guanosine 5'-(gammaS)triphosphate
-
2'-O-[2-(methylamino)benzoyl]guanosine 5'-(gammaS)triphosphate
-
2'-O-[2-(methylamino)benzoyl]guanosine 5'-(gammaS)triphosphate
-
2'-O-[2-(methylamino)benzoyl]guanosine 5'-triphosphate
-
2'-O-[2-(methylamino)benzoyl]guanosine 5'-triphosphate
-
2'-O-[2-(methylamino)benzoyl]guanosine 5'-triphosphate
-
2-hydroxy-5-[(E)-[4-[(pyridin-2-yl)sulfamoyl]phenyl]diazenyl]benzoic acid
-
2-hydroxy-5-[(E)-[4-[(pyridin-2-yl)sulfamoyl]phenyl]diazenyl]benzoic acid
A0A170Y3L9
-
2-hydroxy-5-[(E)-[4-[(pyridin-2-yl)sulfamoyl]phenyl]diazenyl]benzoic acid
-
2-hydroxy-5-[(E)-[4-[(pyridin-2-yl)sulfamoyl]phenyl]diazenyl]benzoic acid
-
2-hydroxy-5-[(E)-[4-[(pyridin-2-yl)sulfamoyl]phenyl]diazenyl]benzoic acid
-
2-hydroxy-5-[(E)-[4-[(pyridin-2-yl)sulfamoyl]phenyl]diazenyl]benzoic acid
-
2-hydroxy-5-[(E)-[4-[(pyridin-2-yl)sulfamoyl]phenyl]diazenyl]benzoic acid
-
3-nitro-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]benzene-1-sulfonohydrazide
85% inhibition at 0.1 mM, competitive binding
3-nitro-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]benzene-1-sulfonohydrazide
-
3-O-alpha-L-rhamnopyranosyl-(1-2)-beta-D-galactopyranosyl-(1-2)-beta-D-glucuronopyranosyl soyasapogenol B 22-O-alpha-D-glucopyranoside
-
-
3-O-alpha-L-rhamnopyranosyl-(1-2)-beta-D-galactopyranosyl-(1-2)-beta-D-glucuronopyranosyl soyasapogenol B 22-O-alpha-D-glucopyranoside
-
noncompetitive, inhibition is decreased by 50% in presence of 0.02 mM cyclic diguanylate, no inhibition in presence of detergents. Inhibitor affects binding of cyclic diguanylate to enzyme. In situ, inhibitor affects bacterial cellulose synthesis and enzyme activity
3-O-alpha-L-rhamnopyranosyl-(1->2)-beta-D-galactopyranosyl-(1->2)-beta-D-glucuronopyranosyl soyasapogenol B 22-O-alpha-D-glucopyranoside
-
3-O-alpha-L-rhamnopyranosyl-(1->2)-beta-D-galactopyranosyl-(1->2)-beta-D-glucuronopyranosyl soyasapogenol B 22-O-alpha-D-glucopyranoside
A0A170Y3L9
-
3-O-alpha-L-rhamnopyranosyl-(1->2)-beta-D-galactopyranosyl-(1->2)-beta-D-glucuronopyranosyl soyasapogenol B 22-O-alpha-D-glucopyranoside
-
3-O-alpha-L-rhamnopyranosyl-(1->2)-beta-D-galactopyranosyl-(1->2)-beta-D-glucuronopyranosyl soyasapogenol B 22-O-alpha-D-glucopyranoside
-
3-O-alpha-L-rhamnopyranosyl-(1->2)-beta-D-galactopyranosyl-(1->2)-beta-D-glucuronopyranosyl soyasapogenol B 22-O-alpha-D-glucopyranoside
-
3-O-alpha-L-rhamnopyranosyl-(1->2)-beta-D-galactopyranosyl-(1->2)-beta-D-glucuronopyranosyl soyasapogenol B 22-O-alpha-D-glucopyranoside
-
3-O-alpha-L-rhamnopyranosyl-(1->2)-beta-D-galactopyranosyl-(1->2)-beta-D-glucuronopyranosyl soyasapogenol B 22-O-alpha-D-glucopyranoside
-
4-(2,5-dimethylphenoxy)-N-(4-morpholin-4-ylphenyl)butanamide
-
4-(2,5-dimethylphenoxy)-N-(4-morpholin-4-ylphenyl)butanamide
A0A170Y3L9
-
4-(2,5-dimethylphenoxy)-N-(4-morpholin-4-ylphenyl)butanamide
-
4-(2,5-dimethylphenoxy)-N-(4-morpholin-4-ylphenyl)butanamide
-
4-(2,5-dimethylphenoxy)-N-(4-morpholin-4-ylphenyl)butanamide
-
4-(2,5-dimethylphenoxy)-N-(4-morpholin-4-ylphenyl)butanamide
-
4-(2,5-dimethylphenoxy)-N-(4-morpholin-4-ylphenyl)butanamide
-
4-chloro-3-nitro-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]benzene-1-sulfonohydrazide
-
4-chloro-3-nitro-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]benzene-1-sulfonohydrazide
A0A170Y3L9
-
4-chloro-3-nitro-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]benzene-1-sulfonohydrazide
-
4-chloro-3-nitro-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]benzene-1-sulfonohydrazide
-
4-chloro-3-nitro-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]benzene-1-sulfonohydrazide
-
4-chloro-3-nitro-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]benzene-1-sulfonohydrazide
-
4-chloro-3-nitro-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]benzene-1-sulfonohydrazide
-
9-(3-[4-[(2-amino-6-chloro-9H-purin-9-yl)methyl]-1H-1,2,3-triazol-1-yl]propyl)-6-chloro-9H-purin-2-amine
-
9-(3-[4-[(2-amino-6-chloro-9H-purin-9-yl)methyl]-1H-1,2,3-triazol-1-yl]propyl)-6-chloro-9H-purin-2-amine
A0A170Y3L9
-
9-(3-[4-[(2-amino-6-chloro-9H-purin-9-yl)methyl]-1H-1,2,3-triazol-1-yl]propyl)-6-chloro-9H-purin-2-amine
-
9-(3-[4-[(2-amino-6-chloro-9H-purin-9-yl)methyl]-1H-1,2,3-triazol-1-yl]propyl)-6-chloro-9H-purin-2-amine
-
9-(3-[4-[(2-amino-6-chloro-9H-purin-9-yl)methyl]-1H-1,2,3-triazol-1-yl]propyl)-6-chloro-9H-purin-2-amine
-
9-(3-[4-[(2-amino-6-chloro-9H-purin-9-yl)methyl]-1H-1,2,3-triazol-1-yl]propyl)-6-chloro-9H-purin-2-amine
-
9-(3-[4-[(2-amino-6-chloro-9H-purin-9-yl)methyl]-1H-1,2,3-triazol-1-yl]propyl)-6-chloro-9H-purin-2-amine
-
c-di-GMP
weak product feedback inhibition is found in PA0847 GGDEF domain suggesting that allosteric regulation from the sensory domain could play a dominant role in the control of intracellular c-di-GMP synthesis
c-di-GMP
feedback inhibition of DGC enzyme GcbC, modelling. In the crystal structure, two molecules of c-di-GMP are found to be bound between the primary and secondary I-sites of this inactive dimer. Three more residues are found to coordinate the formation of the I-site pocket where residue R363 of each monomer of GcbC forms a polar contact with residues E360 and E429 of the other GcbC monomer within the dimer complex of this protein
cyclic di-3',5'-(2'-fluoroguanylate)
-
cyclic di-3',5'-guanylate
noncompetitive product inhibition at an allosteric binding site fully contained within the GGDEF domain. Core of the binding site is an RXXD motif formed by residues R359, D362, and R390
cyclic di-3',5'-guanylate
product inhibition, allosteric feedback regualtion is not affected by the activation state of enzyme
cyclic di-3',5'-guanylate
noncompetitive product inhibition, binding causes crosslinking of diguanylate cyclase (GGDEF) domains within the dimer, integrity of only one inhibitory site required for inhibition
cyclic di-3',5'-guanylate
-
product inhibition, allosteric, negative feedback, slow intrinsic off-rate of cyclic di-3,5-guanylate from RxxD inhibitory-site motif, inhibitory action depends on tetramer formation and subsequent conformational change in dimeric enzyme from global to elongated shape
cyclic di-3',5'-guanylate
-
product inhibition, allosteric, negative feedback, slow intrinsic off-rate of cyclic di-3,5-guanylate from RxxD inhibitory-site motif, inhibitory action depends on tetramer formation and subsequent conformational change in dimeric enzyme from global to elongated shape
cyclic di-3',5'-guanylate
-
product inhibition, allosteric, negative feedback, slow intrinsic off-rate of cyclic di-3,5-guanylate from RxxD inhibitory-site motif, inhibitory action depends on tetramer formation and subsequent conformational change in dimeric enzyme from global to elongated shape
cyclic di-3',5'-guanylate
-
product inhibition, allosteric, negative feedback, slow intrinsic off-rate of cyclic di-3,5-guanylate from RxxD inhibitory-site motif, inhibitory action depends on tetramer formation and subsequent conformational change in dimeric enzyme from global to elongated shape
cyclic di-3',5'-inosinylic acid
-
N'-((1E)-(4-ethoxy-3-[(8-oxo-1,5,6,8-tetrahydro-2H-1,5-methanopyrido[1,2-a][1,5]diazocin-3(4H)-yl)methylphenyl)methylene)]-3,4,5-trihydroxybenzohydrazide
LP3134; LP3134
N'-((1E)-(4-ethoxy-3-[(8-oxo-1,5,6,8-tetrahydro-2H-1,5-methanopyrido[1,2-a][1,5]diazocin-3(4H)-yl)methylphenyl)methylene)]-3,4,5-trihydroxybenzohydrazide
A0A170Y3L9
LP3134
N'-((1E)-(4-ethoxy-3-[(8-oxo-1,5,6,8-tetrahydro-2H-1,5-methanopyrido[1,2-a][1,5]diazocin-3(4H)-yl)methylphenyl)methylene)]-3,4,5-trihydroxybenzohydrazide
LP3134
N'-((1E)-(4-ethoxy-3-[(8-oxo-1,5,6,8-tetrahydro-2H-1,5-methanopyrido[1,2-a][1,5]diazocin-3(4H)-yl)methylphenyl)methylene)]-3,4,5-trihydroxybenzohydrazide
LP3134; LP3134
N'-((1E)-(4-ethoxy-3-[(8-oxo-1,5,6,8-tetrahydro-2H-1,5-methanopyrido[1,2-a][1,5]diazocin-3(4H)-yl)methylphenyl)methylene)]-3,4,5-trihydroxybenzohydrazide
LP3134
N'-((1E)-(4-ethoxy-3-[(8-oxo-1,5,6,8-tetrahydro-2H-1,5-methanopyrido[1,2-a][1,5]diazocin-3(4H)-yl)methylphenyl)methylene)]-3,4,5-trihydroxybenzohydrazide
LP3134
N'-((1E)-(4-ethoxy-3-[(8-oxo-1,5,6,8-tetrahydro-2H-1,5-methanopyrido[1,2-a][1,5]diazocin-3(4H)-yl)methylphenyl)methylene)]-3,4,5-trihydroxybenzohydrazide
LP3134
N'-[(E)-(3,4-dihydroxyphenyl)methylidene]-4-methyl-3-nitrobenzene-1-sulfonohydrazide
-
N'-[(E)-(3,4-dihydroxyphenyl)methylidene]-4-methyl-3-nitrobenzene-1-sulfonohydrazide
83.4% inhibition at 0.1 mM, competitive binding
N'-[(E)-(3,4-dihydroxyphenyl)methylidene]-4-methyl-3-nitrobenzene-1-sulfonohydrazide
A0A170Y3L9
-
N'-[(E)-(3,4-dihydroxyphenyl)methylidene]-4-methyl-3-nitrobenzene-1-sulfonohydrazide
-
N'-[(E)-(3,4-dihydroxyphenyl)methylidene]-4-methyl-3-nitrobenzene-1-sulfonohydrazide
-
N'-[(E)-(3,4-dihydroxyphenyl)methylidene]-4-methyl-3-nitrobenzene-1-sulfonohydrazide
-
N'-[(E)-(3,4-dihydroxyphenyl)methylidene]-4-methyl-3-nitrobenzene-1-sulfonohydrazide
-
N'-[(E)-(3,4-dihydroxyphenyl)methylidene]-4-methyl-3-nitrobenzene-1-sulfonohydrazide
-
N'-[(E)-(3,4-dihydroxyphenyl)methylidene]-4-methyl-3-nitrobenzene-1-sulfonohydrazide
-
N-(((2-phenylethyl)amino)carbonothioyl)benzamide
significantly reduces the total concentration of c-di-GMP in Vibrio cholerae
N-(4-anilinophenyl)benzamide
-
N-(4-anilinophenyl)benzamide
significantly reduces the total concentration of c-di-GMP in Vibrio cholerae
[2- oxo-2-(2-oxopyrrolidin-1-yl)ethyl] 1,3-benzothiazole-6-carboxylate
-
[2- oxo-2-(2-oxopyrrolidin-1-yl)ethyl] 1,3-benzothiazole-6-carboxylate
A0A170Y3L9
-
[2- oxo-2-(2-oxopyrrolidin-1-yl)ethyl] 1,3-benzothiazole-6-carboxylate
-
[2- oxo-2-(2-oxopyrrolidin-1-yl)ethyl] 1,3-benzothiazole-6-carboxylate
-
[2- oxo-2-(2-oxopyrrolidin-1-yl)ethyl] 1,3-benzothiazole-6-carboxylate
-
[2- oxo-2-(2-oxopyrrolidin-1-yl)ethyl] 1,3-benzothiazole-6-carboxylate
-
[2- oxo-2-(2-oxopyrrolidin-1-yl)ethyl] 1,3-benzothiazole-6-carboxylate
-
additional information
screenings for chemicals capable of inhibiting the c-di-GMP synthesis activity of DGCs have been performed in order to inhibit bacterial biofilm formation. 2',3'-O-(2,4,6-trinitrophenyl) (TNP)- and 2' (3')-O-(N-methylanthraniloyl) (MANT)-substituted nucleotides are potent inhibitors of guanylyl and adenylyl cyclases; screenings for chemicals capable of inhibiting the c-di-GMP synthesis activity of DGCs have been performed in order to inhibit bacterial biofilm formation. 2',3'-O-(2,4,6-trinitrophenyl) (TNP)- and 2' (3')-O-(N-methylanthraniloyl) (MANT)-substituted nucleotides are potent inhibitors of guanylyl and adenylyl cyclases
-
additional information
screenings for chemicals capable of inhibiting the c-di-GMP synthesis activity of DGCs have been performed in order to inhibit bacterial biofilm formation. 2',3'-O-(2,4,6-trinitrophenyl) (TNP)- and 2' (3')-O-(N-methylanthraniloyl) (MANT)-substituted nucleotides are potent inhibitors of guanylyl and adenylyl cyclases; screenings for chemicals capable of inhibiting the c-di-GMP synthesis activity of DGCs have been performed in order to inhibit bacterial biofilm formation. 2',3'-O-(2,4,6-trinitrophenyl) (TNP)- and 2' (3')-O-(N-methylanthraniloyl) (MANT)-substituted nucleotides are potent inhibitors of guanylyl and adenylyl cyclases
-
additional information
virtual screening of the ZINC database, in silico discovery and in vitro validation of catechol-containing sulfonohydrazide compounds as potent inhibitors of the diguanylate cyclase PleD. The compounds retrieved from the pharmacophore searches are docked into the active site of PleD, by means of Molegro Virtual Docker (MVD) software (CLCbio), using the three-dimensional structure of PleD (PDB ID 2V0N). Binding of N'-[(E)-(3,4-dihydroxyphenyl)methylidene]-4-methyl-3-nitrobenzene-1-sulfonohydrazide and 3-nitro-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]benzene-1-sulfonohydrazide to PleD is stabilized by polar interactions with residues surrounding the GTP binding pocket, namely, N335, D344, and R366. N'-[(E)-(3,4-dihydroxyphenyl)methylidene]-4-methyl-3-nitrobenzene-1-sulfonohydrazide and 3-nitro-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]benzene-1-sulfonohydrazide share a hydrazine moiety with the previously identified inhibitors LP3134 and LP4010, which has been predicted to interact with the amino group of N335
-
additional information
-
virtual screening of the ZINC database, in silico discovery and in vitro validation of catechol-containing sulfonohydrazide compounds as potent inhibitors of the diguanylate cyclase PleD. The compounds retrieved from the pharmacophore searches are docked into the active site of PleD, by means of Molegro Virtual Docker (MVD) software (CLCbio), using the three-dimensional structure of PleD (PDB ID 2V0N). Binding of N'-[(E)-(3,4-dihydroxyphenyl)methylidene]-4-methyl-3-nitrobenzene-1-sulfonohydrazide and 3-nitro-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]benzene-1-sulfonohydrazide to PleD is stabilized by polar interactions with residues surrounding the GTP binding pocket, namely, N335, D344, and R366. N'-[(E)-(3,4-dihydroxyphenyl)methylidene]-4-methyl-3-nitrobenzene-1-sulfonohydrazide and 3-nitro-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]benzene-1-sulfonohydrazide share a hydrazine moiety with the previously identified inhibitors LP3134 and LP4010, which has been predicted to interact with the amino group of N335
-
additional information
A0A170Y3L9
screenings for chemicals capable of inhibiting the c-di-GMP synthesis activity of DGCs have been performed in order to inhibit bacterial biofilm formation. 2',3'-O-(2,4,6-trinitrophenyl) (TNP)- and 2' (3')-O-(N-methylanthraniloyl) (MANT)-substituted nucleotides are potent inhibitors of guanylyl and adenylyl cyclases
-
additional information
-
the reaction shows non-competitive product inhibition only at comparatively large c-di-GMP concentration
-
additional information
screenings for chemicals capable of inhibiting the c-di-GMP synthesis activity of DGCs have been performed in order to inhibit bacterial biofilm formation. 2',3'-O-(2,4,6-trinitrophenyl) (TNP)- and 2'(3')-O-(N-methylanthraniloyl) (MANT)-substituted nucleotides are potent inhibitors of guanylyl and adenylyl cyclases
-
additional information
screenings for chemicals capable of inhibiting the c-di-GMP synthesis activity of DGCs have been performed in order to inhibit bacterial biofilm formation. 2',3'-O-(2,4,6-trinitrophenyl) (TNP)- and 2' (3')-O-(N-methylanthraniloyl) (MANT)-substituted nucleotides are potent inhibitors of guanylyl and adenylyl cyclases; screenings for chemicals capable of inhibiting the c-di-GMP synthesis activity of DGCs have been performed in order to inhibit bacterial biofilm formation. 2',3'-O-(2,4,6-trinitrophenyl) (TNP)- and 2'(3')-O-(N-methylanthraniloyl) (MANT)-substituted nucleotides are potent inhibitors of guanylyl and adenylyl cyclases
-
additional information
screenings for chemicals capable of inhibiting the c-di-GMP synthesis activity of DGCs have been performed in order to inhibit bacterial biofilm formation. 2',3'-O-(2,4,6-trinitrophenyl) (TNP)- and 2' (3')-O-(N-methylanthraniloyl) (MANT)-substituted nucleotides are potent inhibitors of guanylyl and adenylyl cyclases; screenings for chemicals capable of inhibiting the c-di-GMP synthesis activity of DGCs have been performed in order to inhibit bacterial biofilm formation. 2',3'-O-(2,4,6-trinitrophenyl) (TNP)- and 2'(3')-O-(N-methylanthraniloyl) (MANT)-substituted nucleotides are potent inhibitors of guanylyl and adenylyl cyclases
-
additional information
enzyme PA0847 demonstrates no significant product inhibition, though the key residues of two I-sites for c-di-GMP binding are conserved in its GGDEF domain. ENzyme PA0847 contains the canonical product inhibition site (primary I site) of the RxxD motif, which is located upstream of the conserved GGDEF motif. It also has a secondary inhibition site which is conserved in GGDEF domains that can undergo feedback inhibition. These two sites may form a pocket for c-di-GMP binding
-
additional information
virtual screening of the ZINC database, in silico discovery and in vitro validation of catechol-containing sulfonohydrazide compounds as potent inhibitors of the diguanylate cyclase PleD. N'-[(E)-(3,4-dihydroxyphenyl)methylidene]-4-methyl-3-nitrobenzene-1-sulfonohydrazide and 3-nitro-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]benzene-1-sulfonohydrazide are also tested on the YfiNHAMP-GGDEF and WspR DGCs from Pseudomonas aeruginosa, two DGCs which are in the on state and therefore do not require preactivation; virtual screening of the ZINC database, in silico discovery and in vitro validation of catechol-containing sulfonohydrazide compounds as potent inhibitors of the diguanylate cyclase PleD. N'-[(E)-(3,4-dihydroxyphenyl)methylidene]-4-methyl-3-nitrobenzene-1-sulfonohydrazide and 3-nitro-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]benzene-1-sulfonohydrazide are also tested on the YfiNHAMP-GGDEF and WspR DGCs from Pseudomonas aeruginosa, two DGCs which are in the on state and therefore do not require preactivation
-
additional information
virtual screening of the ZINC database, in silico discovery and in vitro validation of catechol-containing sulfonohydrazide compounds as potent inhibitors of the diguanylate cyclase PleD. N'-[(E)-(3,4-dihydroxyphenyl)methylidene]-4-methyl-3-nitrobenzene-1-sulfonohydrazide and 3-nitro-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]benzene-1-sulfonohydrazide are also tested on the YfiNHAMP-GGDEF and WspR DGCs from Pseudomonas aeruginosa, two DGCs which are in the on state and therefore do not require preactivation; virtual screening of the ZINC database, in silico discovery and in vitro validation of catechol-containing sulfonohydrazide compounds as potent inhibitors of the diguanylate cyclase PleD. N'-[(E)-(3,4-dihydroxyphenyl)methylidene]-4-methyl-3-nitrobenzene-1-sulfonohydrazide and 3-nitro-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]benzene-1-sulfonohydrazide are also tested on the YfiNHAMP-GGDEF and WspR DGCs from Pseudomonas aeruginosa, two DGCs which are in the on state and therefore do not require preactivation
-
additional information
GcbC has a primary inhibitory site with the previously characterized RXXD motif. The RXXD motif is found at residues R410 to D413 of GcbC. Residue R409 also makes contact with a c-di-GMP molecule. In addition to the primary I-site, GcbC also contains a secondary I-site at position R366 that completes GcbC's regulatory c-di-GMP binding site. The autoinhibitory site (I-site) of a diguanylate cyclase is a necessary element for interaction and signaling with an effector protein
-
additional information
-
GcbC has a primary inhibitory site with the previously characterized RXXD motif. The RXXD motif is found at residues R410 to D413 of GcbC. Residue R409 also makes contact with a c-di-GMP molecule. In addition to the primary I-site, GcbC also contains a secondary I-site at position R366 that completes GcbC's regulatory c-di-GMP binding site. The autoinhibitory site (I-site) of a diguanylate cyclase is a necessary element for interaction and signaling with an effector protein
-
additional information
screenings for chemicals capable of inhibiting the c-di-GMP synthesis activity of DGCs have been performed in order to inhibit bacterial biofilm formation. 2',3'-O-(2,4,6-trinitrophenyl) (TNP)- and 2' (3')-O-(N-methylanthraniloyl) (MANT)-substituted nucleotides are potent inhibitors of guanylyl and adenylyl cyclases
-
additional information
screenings for chemicals capable of inhibiting the c-di-GMP synthesis activity of DGCs have been performed in order to inhibit bacterial biofilm formation. 2',3'-O-(2,4,6-trinitrophenyl) (TNP)- and 2'(3')-O-(N-methylanthraniloyl) (MANT)-substituted nucleotides are potent inhibitors of guanylyl and adenylyl cyclases
-
additional information
screenings for chemicals capable of inhibiting the c-di-GMP synthesis activity of DGCs have been performed in order to inhibit bacterial biofilm formation. 2',3'-O-(2,4,6-trinitrophenyl) (TNP)- and 2' (3')-O-(N-methylanthraniloyl) (MANT)-substituted nucleotides are potent inhibitors of guanylyl and adenylyl cyclases
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4-(5-[(E)-[2-(4-amino-1,2,5-oxadiazole-3-carbonyl)hydrazinylidene]methyl]furan-2-yl)benzoic acid
18% activation at 0.1 mM
4-chloro-N'-[(E)-(4-cyanophenyl)methylidene]-3-nitrobenzene-1-sulfonohydrazide
15% activation at 0.1 mM
4-[(E)-[2-(4-hydroxy-6-methylpyrimidin-2-yl)hydrazinylidene]methyl]phenyl 3-nitrobenzoate
8% activation at 0.1 mM
4-[(E)-[2-(4-sulfamoylphenyl)hydrazinylidene]methyl]benzoic acid
6% activation at 0.1 mM
cAMP
required, Lcd1 DGC activity is negligible in the absence of cAMP and is significantly enhanced in its presence. The GAF domain binds specifically cAMP and has an important role in the regulation of the DGC activity of the GGDEF domain. cAMP binding site and specificity, overview
N'-[(E)-(4-chloro-3-nitrophenyl)methylidene]-4-methyl-3-nitrobenzene-1-sulfonohydrazide
3% activation at 0.1 mM
N'-[(E)-(4-cyanophenyl)methylidene]-4-methyl-3-nitrobenzene-1-sulfonohydrazide
4% activation at 0.1 mM
paraquat
enhances DgcZ-dependent biofilm formation in an FRD-dependent fashion
beryllium fluoride
BeF3-, pseudo-phosphorylation, enhances dimerisation by lowering KD to less than 10 microM, tightens dimer interface between two D1/D2 domains, modification activates enzyme
beryllium fluoride
BeF3, phosphoryl mimic, optimum concentration: 1 mM BeCl2/10 mM NaF (nonspecifcally inhibitory at higher concentrations), causes dimerisation and cyclic di-3,5-guanylate synthesis, no influence on cyclic-di-GMP binding affinity and thus allosteric regulation
additional information
PleD contains an extra metal binding site or beryllium metal for activation
-
additional information
-
PleD contains an extra metal binding site or beryllium metal for activation
-
additional information
membrane association of SadC promotes its DGC activity by affecting the formation of active DGC oligomers
-
additional information
-
membrane association of SadC promotes its DGC activity by affecting the formation of active DGC oligomers
-
additional information
-
oligomerization-dependent activation of WspR, the stalks are key regulatory elements for the oligomerization, activation, and autoinhibition of WspR
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Enteritis
Necrotic enteritis locus 1 diguanylate cyclase and phosphodiesterase (cyclic-di-GMP) gene mutation attenuates virulence in an avian necrotic enteritis isolate of Clostridium perfringens.
Infections
Bordetella bronchiseptica Diguanylate Cyclase BdcA Regulates Motility and Is Important for the Establishment of Respiratory Infection in Mice.
Infections
Chp8, a diguanylate cyclase from Pseudomonas syringae pv. Tomato DC3000, suppresses the pathogen-associated molecular pattern flagellin, increases extracellular polysaccharides, and promotes plant immune evasion.
Infections
Evaluation of a Salmonella Strain Lacking the Secondary Messenger C-di-GMP and RpoS as a Live Oral Vaccine.
Infections
Membrane association of SadC enhances its diguanylate cyclase activity to control exopolysaccharides synthesis and biofilm formation in Pseudomonas aeruginosa.
Infections
The Anaplasma phagocytophilum PleC histidine kinase and PleD diguanylate cyclase two-component system and role of cyclic Di-GMP in host cell infection.
Infections
The Nitrite Transporter Facilitates Biofilm Formation via Suppression of Nitrite Reductase and Is a New Antibiofilm Target in Pseudomonas aeruginosa.
Lyme Disease
The diguanylate cyclase, Rrp1, regulates critical steps in the enzootic cycle of the Lyme disease spirochetes.
Tuberculosis
Diguanylate cyclase activity of the Mycobacterium leprae T cell antigen ML1419c.
Whooping Cough
Globins synthesize the second messenger bis-(3'-5')-cyclic diguanosine monophosphate in bacteria.
Whooping Cough
The importance of conserved amino acids in heme-based globin-coupled diguanylate cyclases.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.025
cyclic di-3',5'-guanylate
triple mutant R148A/R178A/R313A
0.022
GTP
enzyme with 5-coordinate Fe(III) heme mutant L65G, pH 8.0, 24°C
0.029
GTP
enzyme with 5-coordinate Fe(III) heme mutant Y43F, pH 8.0, 24°C
0.038
GTP
Q8PPS5
mutant K759A, Michaelis-Menten model, pH 8.0, 30°C
0.042
GTP
enzyme with 5-coordinate Fe(III) heme mutant L65M, pH 8.0, 24°C
0.054
GTP
enzyme with 5-coordinate Fe(III) heme mutant Y43A, pH 8.0, 24°C
0.063
GTP
enzyme with 5-coordinate Fe(III) heme mutant L65T, pH 8.0, 24°C
0.084
GTP
wild-type enzyme with 5-coordinate Fe(III) heme, pH 8.0, 24°C
0.101
GTP
enzyme with 5-coordinate Fe(III) heme mutant L65Q, pH 8.0, 24°C
additional information
additional information
Michaelis-Menten kinetics, kinetic analysis
-
additional information
additional information
-
Michaelis-Menten kinetics, kinetic analysis
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00081
cyclic di-3',5'-guanylate
triple mutant R148A/R178A/R313A, inhibited
0.016
cyclic di-3',5'-guanylate
triple mutant R148A/R178A/R313A
0.0025
GTP
enzyme with 5-coordinate Fe(III) heme mutant L65G, pH 8.0, 24°C
0.0043
GTP
enzyme with 5-coordinate Fe(III) heme mutant L65Q, pH 8.0, 24°C
0.005
GTP
enzyme with mutant 5-coordinate Fe(II)-CO heme, pH 8.0, 24°C
0.009
GTP
enzyme with 5-coordinate Fe(III) heme mutant Y43A, pH 8.0, 24°C
0.0115
GTP
enzyme with 5-coordinate Fe(III) heme mutant Y43F, pH 8.0, 24°C
0.014
GTP
Q8PPS5
mutant K759A, Michaelis-Menten model, pH 8.0, 30°C
0.015
GTP
enzyme with 5-coordinate Fe(III) heme mutant L65M, pH 8.0, 24°C
0.016
GTP
enzyme with mutant 5-coordinate Fe(II)-O2 heme, pH 8.0, 24°C
0.078
GTP
enzyme with 5-coordinate Fe(III) heme mutant L65T, pH 8.0, 24°C
0.13
GTP
in presence of cAMP, pH 8.0, 30°C
additional information
cyclic di-3',5'-guanylate
-
wild-type, inhibited, no activity detected
additional information
cyclic di-3',5'-guanylate
wild-type, inhibited, no activity detected
additional information
cyclic di-3',5'-guanylate
-
double mutant R148A/R178A, inhibited, no activity detected
additional information
cyclic di-3',5'-guanylate
double mutant R148A/R178A, inhibited, no activity detected
additional information
cyclic di-3',5'-guanylate
-
mutant R313A, inhibited, no activity detected
additional information
cyclic di-3',5'-guanylate
mutant R313A, inhibited, no activity detected
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.043
GTP
enzyme with 5-coordinate Fe(III) heme mutant L65Q, pH 8.0, 24°C
0.114
GTP
enzyme with 5-coordinate Fe(III) heme mutant L65G, pH 8.0, 24°C
0.167
GTP
enzyme with 5-coordinate Fe(III) heme mutant Y43A, pH 8.0, 24°C
0.357
GTP
enzyme with 5-coordinate Fe(III) heme mutant L65M, pH 8.0, 24°C
0.397
GTP
enzyme with 5-coordinate Fe(III) heme mutant Y43F, pH 8.0, 24°C
1.238
GTP
enzyme with 5-coordinate Fe(III) heme mutant L65T, pH 8.0, 24°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.005
3-O-alpha-L-rhamnopyranosyl-(1-2)-beta-D-galactopyranosyl-(1-2)-beta-D-glucuronopyranosyl soyasapogenol B 22-O-alpha-D-glucopyranoside
-
pH 7.5, 30°C
0.0029
cyclic di-3',5'-guanylate
mutant R148A/R178A, 30°C, pH 8.0
0.033
cyclic di-3',5'-guanylate
triple mutant R148A/R178A/R313A
0.1
cyclic di-3',5'-guanylate
or above, mutant R359A, 30°C, pH 8.0
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0001
2',3'-O-[2,4,6-trinitrocyclohexa-2,5-diene-1,1-diyl]-GTP
Escherichia coli
-
pH 8, 30°C
0.01107
3-nitro-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]benzene-1-sulfonohydrazide
Caulobacter vibrioides
pH 7.5, 22°C
0.005
3-O-alpha-L-rhamnopyronosyl-(1->2)-beta-D-galactopyranosyl-(1->2)-beta-D-gluconopyranosyl soyasapogenol B 22-o-alpha-D-glucopyranoside
Komagataeibacter xylinus
pH and temperature not specified in the publication
0.01105
N'-[(E)-(3,4-dihydroxyphenyl)methylidene]-4-methyl-3-nitrobenzene-1-sulfonohydrazide
Caulobacter vibrioides
pH 7.5, 22°C
0.011
cyclic di-3',5'-(2'-fluoroguanylate)
Pseudomonas aeruginosa
pH and temperature not specified in the publication
0.1
cyclic di-3',5'-(2'-fluoroguanylate)
Synechocystis sp. PCC 6803
about, pH and temperature not specified in the publication
0.0122
N-(((2-phenylethyl)amino)carbonothioyl)benzamide
Pseudomonas aeruginosa
-
pH 7.5, 20°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.000036
mutant Y26A, in presence of BeF3 (1 mM BeCl2, 10 mM NaF)
0.00004
mutant Y26A in presence of beryllium trifluoride, pH 7.8
0.0011
0.16
additional information
0.0011
mutant D53N in presence of beryllium trifluoride, pH 7.8
0.0011
mutant D53N, in presence of BeF3 (1 mM BeCl2, 10 mM NaF)
additional information
-
increased activity in presence of phosphodiesterases through hydrolysis of cyclic di-3,5-guanylate thus reduction of product inhibition
additional information
-
increased activity in presence of phosphodiesterases through hydrolysis of cyclic di-3,5-guanylate thus reduction of product inhibition
additional information
-
increased activity in presence of phosphodiesterases through hydrolysis of cyclic di-3,5-guanylate thus reduction of product inhibition
additional information
-
increased activity in presence of phosphodiesterases through hydrolysis of cyclic di-3,5-guanylate thus reduction of product inhibition
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 10
the enzyme is inactive below pH 6.0 and above pH 10.0, optimal pH at pH 8.5-9.00, 50% of maximal activity at pH 7.0, 80% of maximal activity at pH 8.0
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20
22
30
37
55
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
bi-functional enzyme with cyclase and phosphodiesterase functions
-
-
brenda
Peptoclostridium difficile or Clostridium difficile
A0A170Y3L9
UniProt
brenda
Gluconoacetobacter xylinus or Acetobacter xylinum
UniProt
brenda
isoforms Cdg1, Cdg2, Cdg3. Cdg1 contributes 80% of cellular enzymic activites, Cdg2 and Cdg3 contribute 15 and 5%, resp.
-
-
brenda
strain PA14, gene PA4367 encodes a protein with an EAL domain associated with cyclic di-3'5'-guanylate phosphodiesterase activity, and a DDGEF domain associated with cyclic di-di-3'5'-guanylate cyclase activity
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
heterocyst differentiation pathway (upstream of HetR), decreased heterocyst frequency and block of heterocyst differentiation within 4 days in mutant strain depleted for all2874 gene and grown in absence of source of combined nitrogen
brenda
additional information
additional information
quantitative reverse transcription-PCR (qRT-PCR) confirms the increase in transcript abundance of PA3177 to be 6.5fold in biofilm cells relative to planktonic cells
brenda
additional information
-
quantitative reverse transcription-PCR (qRT-PCR) confirms the increase in transcript abundance of PA3177 to be 6.5fold in biofilm cells relative to planktonic cells
brenda
additional information
-
quantitative reverse transcription-PCR (qRT-PCR) confirms the increase in transcript abundance of PA3177 to be 6.5fold in biofilm cells relative to planktonic cells
-
brenda
additional information
-
quantitative reverse transcription-PCR (qRT-PCR) confirms the increase in transcript abundance of PA3177 to be 6.5fold in biofilm cells relative to planktonic cells
-
brenda
additional information
-
quantitative reverse transcription-PCR (qRT-PCR) confirms the increase in transcript abundance of PA3177 to be 6.5fold in biofilm cells relative to planktonic cells
-
brenda
additional information
-
quantitative reverse transcription-PCR (qRT-PCR) confirms the increase in transcript abundance of PA3177 to be 6.5fold in biofilm cells relative to planktonic cells
-
brenda
additional information
-
quantitative reverse transcription-PCR (qRT-PCR) confirms the increase in transcript abundance of PA3177 to be 6.5fold in biofilm cells relative to planktonic cells
-
brenda
additional information
-
quantitative reverse transcription-PCR (qRT-PCR) confirms the increase in transcript abundance of PA3177 to be 6.5fold in biofilm cells relative to planktonic cells
-
brenda
additional information
-
quantitative reverse transcription-PCR (qRT-PCR) confirms the increase in transcript abundance of PA3177 to be 6.5fold in biofilm cells relative to planktonic cells
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
response regulator PleD-GFP protein specifically localizes to the stalked pole and is absent from the flagellated swarmer pole. Targeting of PleD to the cell pole is coupled to the activation of its C-terminal di-guanylate cyclase domain
brenda
recruitment to predivisional pole during cell cycle of differentiating cells dependends on dimerisation
brenda
polar localization of DgcZ is independent of protein activity and concentration. Polar localization of DgcZ is induced by carbon starvation and alkaline pH
brenda
HsbD localizes at the cell pole. HsbD and FlhF colocalize transiently at the pole
brenda
-
HsbD localizes at the cell pole. HsbD and FlhF colocalize transiently at the pole
-
brenda
SadC and RoeA are differently localized
-
brenda
SadC is an inner membrane protein, which is predicted to have five transmembrane domains at N-terminal and a GGDEF domain at C-terminal. Membrane association of SadC promotes its DGC activity by affecting the formation of active DGC oligomers
-
brenda
-
SadC is an inner membrane protein, which is predicted to have five transmembrane domains at N-terminal and a GGDEF domain at C-terminal. Membrane association of SadC promotes its DGC activity by affecting the formation of active DGC oligomers
-
-
brenda
-
SadC is an inner membrane protein, which is predicted to have five transmembrane domains at N-terminal and a GGDEF domain at C-terminal. Membrane association of SadC promotes its DGC activity by affecting the formation of active DGC oligomers
-
-
brenda
-
SadC is an inner membrane protein, which is predicted to have five transmembrane domains at N-terminal and a GGDEF domain at C-terminal. Membrane association of SadC promotes its DGC activity by affecting the formation of active DGC oligomers
-
-
brenda
-
SadC is an inner membrane protein, which is predicted to have five transmembrane domains at N-terminal and a GGDEF domain at C-terminal. Membrane association of SadC promotes its DGC activity by affecting the formation of active DGC oligomers
-
-
brenda
-
SadC is an inner membrane protein, which is predicted to have five transmembrane domains at N-terminal and a GGDEF domain at C-terminal. Membrane association of SadC promotes its DGC activity by affecting the formation of active DGC oligomers
-
-
brenda
-
SadC is an inner membrane protein, which is predicted to have five transmembrane domains at N-terminal and a GGDEF domain at C-terminal. Membrane association of SadC promotes its DGC activity by affecting the formation of active DGC oligomers
-
-
brenda
-
SadC is an inner membrane protein, which is predicted to have five transmembrane domains at N-terminal and a GGDEF domain at C-terminal. Membrane association of SadC promotes its DGC activity by affecting the formation of active DGC oligomers
-
-
brenda
-
isoform Dgc1 has two possible transmembrane helices and Dgc2 has one
brenda
protein harbors 10 predicted C-terminal transmembrane domains
brenda
-
protein harbors 10 predicted C-terminal transmembrane domains
-
brenda
domain analysis of PA0847 shows a unique molecular architecture with an N-terminal periplasmic sensory domain and a C-terminal intracellular GGDEF domain
brenda
-
domain analysis of PA0847 shows a unique molecular architecture with an N-terminal periplasmic sensory domain and a C-terminal intracellular GGDEF domain
-
brenda
-
domain analysis of PA0847 shows a unique molecular architecture with an N-terminal periplasmic sensory domain and a C-terminal intracellular GGDEF domain
-
brenda
-
domain analysis of PA0847 shows a unique molecular architecture with an N-terminal periplasmic sensory domain and a C-terminal intracellular GGDEF domain
-
brenda
-
domain analysis of PA0847 shows a unique molecular architecture with an N-terminal periplasmic sensory domain and a C-terminal intracellular GGDEF domain
-
brenda
-
domain analysis of PA0847 shows a unique molecular architecture with an N-terminal periplasmic sensory domain and a C-terminal intracellular GGDEF domain
-
brenda
-
domain analysis of PA0847 shows a unique molecular architecture with an N-terminal periplasmic sensory domain and a C-terminal intracellular GGDEF domain
-
brenda
-
domain analysis of PA0847 shows a unique molecular architecture with an N-terminal periplasmic sensory domain and a C-terminal intracellular GGDEF domain
-
brenda
-
AdrA is a predicted membrane protein with a putative sensory domain
brenda
-
AdrA is a predicted membrane protein with a putative sensory domain
-
brenda
-
membrane topology with 6 transmembrane segments and 6 cytoplasmic loops, overview
brenda
-
membrane topology with 6 transmembrane segments and 6 cytoplasmic loops, overview
-
brenda
both PBPb-I domains are membrane-distal with the pockets oriented relatively upwards, and both PBPb-II domains are membrane-proximal with the pockets relatively downwards. The two C-terminal alpha8' helices serving as pre-transmembrane sequences at the membrane-proximal end of the structure locate adjacent to each one and can be connected to the subsequent transmembrane helices
brenda
-
both PBPb-I domains are membrane-distal with the pockets oriented relatively upwards, and both PBPb-II domains are membrane-proximal with the pockets relatively downwards. The two C-terminal alpha8' helices serving as pre-transmembrane sequences at the membrane-proximal end of the structure locate adjacent to each one and can be connected to the subsequent transmembrane helices
-
brenda
-
both PBPb-I domains are membrane-distal with the pockets oriented relatively upwards, and both PBPb-II domains are membrane-proximal with the pockets relatively downwards. The two C-terminal alpha8' helices serving as pre-transmembrane sequences at the membrane-proximal end of the structure locate adjacent to each one and can be connected to the subsequent transmembrane helices
-
brenda
additional information
nutrient starvation or the accumulation of byproducts in the medium may result in polar localization of DgcZ in stationary phase. Restoring nutrient-sufficient conditions results in decreased levels and dispersed localization of DgcZ
-
brenda
additional information
-
nutrient starvation or the accumulation of byproducts in the medium may result in polar localization of DgcZ in stationary phase. Restoring nutrient-sufficient conditions results in decreased levels and dispersed localization of DgcZ
-
brenda
additional information
HptB affects the overall distribution of HsbD localization. The frequency of cells exhibiting HsbDC-ter-YFP at both cell poles is significantly increased in a hptB mutant
-
brenda
additional information
-
HptB affects the overall distribution of HsbD localization. The frequency of cells exhibiting HsbDC-ter-YFP at both cell poles is significantly increased in a hptB mutant
-
brenda
additional information
-
HptB affects the overall distribution of HsbD localization. The frequency of cells exhibiting HsbDC-ter-YFP at both cell poles is significantly increased in a hptB mutant
-
-
brenda
additional information
the periplasmic portion comprises residues 46-491. The periplasmic portion of CdgH forms a dimer in solution, L-arginine binding causes conformational changes of the dimer, structure overview. The architecture of the periplasmic tandem PBPb domains of CdgH may undergo a conformational changes from loose dimer to compact dimer
-
brenda
additional information
-
the periplasmic portion comprises residues 46-491. The periplasmic portion of CdgH forms a dimer in solution, L-arginine binding causes conformational changes of the dimer, structure overview. The architecture of the periplasmic tandem PBPb domains of CdgH may undergo a conformational changes from loose dimer to compact dimer
-
-
brenda
additional information
-
the periplasmic portion comprises residues 46-491. The periplasmic portion of CdgH forms a dimer in solution, L-arginine binding causes conformational changes of the dimer, structure overview. The architecture of the periplasmic tandem PBPb domains of CdgH may undergo a conformational changes from loose dimer to compact dimer
-
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
the GGDEF domain of HsbD has the conserved RxxDmotif (293-296 aa), which forms the allosteric inhibitory site (I-site) of diguanylate cyclases
evolution
proteins with a conserved C-terminal GGDEF domain act as DGCs, whereas proteins containing EAL or HD-GYP domains act as c-di-GMP-specific phosphodiesterases (PDEs). Vibrio cholerae genome typically encodes 31 proteins with a GGDEF domain
evolution
close LIC13137 orthologues, with more than 23% identity, are exclusively found in pathogenic species of the Leptospira genus
evolution
Pseudomonas putida strain KT2440 has dozens of DGC/PDE-encoding genes in its genome. GcsA homologues are also found in strains of several other Pseudomonas species, including Pseudomonas monteilii strain SB3078, Pseudomonas plecoglossicida strain NyZ12, and Pseudomonas cremoricolorata strain ND07, which share more than 79% amino acid sequence identity with one another, but no GcsA homologues are found in the model organisms Pseudomonas aeruginosa strains PAO1 and PA14, Pseudomonas fluorescens strain Pfl5, and Pseudomonas syringae pv. tomato strain DC3000
evolution
-
the GGDEF domain of HsbD has the conserved RxxDmotif (293-296 aa), which forms the allosteric inhibitory site (I-site) of diguanylate cyclases
-
evolution
-
Pseudomonas putida strain KT2440 has dozens of DGC/PDE-encoding genes in its genome. GcsA homologues are also found in strains of several other Pseudomonas species, including Pseudomonas monteilii strain SB3078, Pseudomonas plecoglossicida strain NyZ12, and Pseudomonas cremoricolorata strain ND07, which share more than 79% amino acid sequence identity with one another, but no GcsA homologues are found in the model organisms Pseudomonas aeruginosa strains PAO1 and PA14, Pseudomonas fluorescens strain Pfl5, and Pseudomonas syringae pv. tomato strain DC3000
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evolution
-
Pseudomonas putida strain KT2440 has dozens of DGC/PDE-encoding genes in its genome. GcsA homologues are also found in strains of several other Pseudomonas species, including Pseudomonas monteilii strain SB3078, Pseudomonas plecoglossicida strain NyZ12, and Pseudomonas cremoricolorata strain ND07, which share more than 79% amino acid sequence identity with one another, but no GcsA homologues are found in the model organisms Pseudomonas aeruginosa strains PAO1 and PA14, Pseudomonas fluorescens strain Pfl5, and Pseudomonas syringae pv. tomato strain DC3000
-
evolution
-
Pseudomonas putida strain KT2440 has dozens of DGC/PDE-encoding genes in its genome. GcsA homologues are also found in strains of several other Pseudomonas species, including Pseudomonas monteilii strain SB3078, Pseudomonas plecoglossicida strain NyZ12, and Pseudomonas cremoricolorata strain ND07, which share more than 79% amino acid sequence identity with one another, but no GcsA homologues are found in the model organisms Pseudomonas aeruginosa strains PAO1 and PA14, Pseudomonas fluorescens strain Pfl5, and Pseudomonas syringae pv. tomato strain DC3000
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evolution
-
proteins with a conserved C-terminal GGDEF domain act as DGCs, whereas proteins containing EAL or HD-GYP domains act as c-di-GMP-specific phosphodiesterases (PDEs). Vibrio cholerae genome typically encodes 31 proteins with a GGDEF domain
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evolution
-
proteins with a conserved C-terminal GGDEF domain act as DGCs, whereas proteins containing EAL or HD-GYP domains act as c-di-GMP-specific phosphodiesterases (PDEs). Vibrio cholerae genome typically encodes 31 proteins with a GGDEF domain
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malfunction
a deletion mutant shows a marked reduction in biofilm formation
malfunction
deletion mutant shows a biofilm formation defect, a better swarming motility and a significant reduction of c-di-GMP levels. No correlation between leveles of c-di-GMP and the observed phenotypic output with regard to swarming motilities and extracellular polysaccharide (EPS) is observed
malfunction
double mutant containing a deleted sadC and PA1107 gene show a more severe biofilm defect compared to single mutant
malfunction
over-expression of PA1107 leads to enhanced c-di-GMP levels
malfunction
deletion mutant shows a biofilm formation defect, a 4fold better swarming motility and a significant reduction of c-di-GMP levels. No correlation between leveles of c-di-GMP and the observed phenotypic output with regard to swarming motilities and extracellular polysaccharide (EPS) is observed
malfunction
-
heterologous expression of cdgB in Escherichia coli results in increased production of extracellular matrix in colonies and enhanced surface attachment of cells in standing liquid cultures. In Streptomyces coelicolor, both overexpression and deletion of cdgB inhibits aerial-mycelium formation, and overexpression also inhibits production of the antibiotic actinorhodin, implicating c-di-GMP in the regulation of developmental processes in Streptomyces
malfunction
-
overexpression of YddV stimulates production of poly-N-acetylglucosamine (PNAG), an extracellular polysaccharaide able to promote biofilm formation, by triggering expression of pgaABCD, the PNAG biosynthetic operon
malfunction
-
Borrelia burgdorferi strains that lack Rrp1 or that constitutively produce elevated levels of Rrp1 are generated and analyzed for their ability to infect and transit between mice and Ixodes ticks. Rrp1, and by extension, c-di-GMP, are not required for murine infection, but are required for the successful establishment of a productive population of Borrelia burgdorferi in ticks
malfunction
enzyme inhibition by inhibitors causes inhibition of biofilm formation of the organism
malfunction
the inactive heme-free H93A mutant is primarily octameric, suggesting that catalytically active dimer formation requires heme binding
malfunction
-
deletion of hns or rsmB in the gcpAD418A site-directed mutant restored its Pel production and pelD expression, demonstrating that H-NS and RsmB contribute to the GcpA-dependent regulation of Pel in Dickeya dadantii
malfunction
inactivation of PA3177 renders Pseudomonas aeruginosa strain PAO1 biofilms susceptible to tobramycin and hydrogen peroxide. Inactivation of PA3177 also eliminates the recalcitrance of biofilms to killing by tobramycin, with multicopy expression of PA3177 but not PA3177_GGAAF harboring substitutions in the active site, restoring tolerance to wild-type levels. While PA3177 contributes to biofilm drug tolerance, inactivation of PA3177 has no effect on attachment and biofilm formation. Inactivation of PA3177 correlates with reduced c-di-GMP levels in biofilm but not planktonic cells. Inactivation of PA3177 has no effect on attachment and the formation of mature biofilms characterized by a three-dimensional biofilm architecture
malfunction
overexpression of SadC in Pseudomonas aeruginosa strain PAO1 totally inhibits swimming motility and significantly enhances the production of exopolysaccharide Psl. SadC lacking transmembrane domains (SadC300-487) cannot localize on cytoplasmic membrane and form cluster, loses the ability to inhibit the swimming and twitching motility, and shows the attenuated activity to promote Psl production despite that SadC300-487 is able to catalyze the synthesize of c-di-GMP in vitro and in vivo. Truncated enzyme version SadC300-487 can catalyze the synthesis of c-di-GMP in vitro, but version SadC323-487 cannot, structure-function analysis, overview
malfunction
weak product feedback inhibition is found in PA0847 GGDEF domain suggesting that allosteric regulation from the sensory domain could play a dominant role in the control of intracellular c-di-GMP synthesis
malfunction
nutrient starvation or the accumulation of byproducts in the medium may result in polar localization of DgcZ in stationary phase. Restoring nutrient-sufficient conditions results in decreased levels and dispersed localization of DgcZ
malfunction
mutation of residues at the I-site of a DGC disrupts the interaction with its target receptor. By creating various substitutions to a DGC's I-site, it is shown that signaling between a DGC (GcbC) and its target protein (LapD) is a combined function of the I-site-dependent protein-protein interaction and the level of c-di-GMP production. Disruption of the I-site of GcbC leads to deregulation of c-di-GMP production, an increase in the c-di-GMP level and a concomitant increase in c-di-GMP-regulated processes
malfunction
mutation of gene slr1143 results in an aberrant phototactic behaviour in red light. DELTAslr1143 and Slr1143 overexpression mutant lines in different light qualities suggesting that motility of Synechocystis cells can be affected by the cellular levels of c-di-GMP, but this appears to not be the exclusive reason for differences in motility
malfunction
enzyme inhibition by inhibitors causes inhibition of biofilm formation of the organism
malfunction
-
overexpression of cdgH results in a high amount of c-di-GMP accumulation in the cell
malfunction
the CdgD deletion mutant shows significant alteration in the biofilm formation compared to wild-type. Deletion of cdgD causes an increase in motility
malfunction
mutations at the central positions of the GGEEF sequence are detrimental to the functional activity of the enzyme. This DGC lacks the site for allosteric inhibition found in the other DGCs of Vibrio cholerae, suggesting a different mode of inhibitory control in this DGC
malfunction
BpeGReg266 (residues 1-266) and BpeGReg296 (residues 1-296), which only contain the globin and middle domains, can inhibit bacterial motility. The distal residues of the globin domain affect diguanylate cyclase activity, Bpe-GReg may interact with other c-di-GMP-metabolizing proteins to form mixed signaling teams
malfunction
mutation in the GGDEF motif (from GGDEF to GGAAF) abolishes the c-di-GMP synthesis ability of GcsA
malfunction
A0A170Y3L9
enzyme inhibition by inhibitors causes inhibition of biofilm formation of the organism
malfunction
enzyme inhibition by inhibitors causes inhibition of biofilm formation of the organism
malfunction
enzyme inhibition by inhibitors causes inhibition of biofilm formation of the organism
malfunction
enzyme inhibition by inhibitors causes inhibition of biofilm formation of the organism
malfunction
enzyme inhibition by inhibitors causes inhibition of biofilm formation of the organism
malfunction
-
BpeGReg266 (residues 1-266) and BpeGReg296 (residues 1-296), which only contain the globin and middle domains, can inhibit bacterial motility. The distal residues of the globin domain affect diguanylate cyclase activity, Bpe-GReg may interact with other c-di-GMP-metabolizing proteins to form mixed signaling teams
-
malfunction
-
enzyme inhibition by inhibitors causes inhibition of biofilm formation of the organism
-
malfunction
-
deletion of hns or rsmB in the gcpAD418A site-directed mutant restored its Pel production and pelD expression, demonstrating that H-NS and RsmB contribute to the GcpA-dependent regulation of Pel in Dickeya dadantii
-
malfunction
-
mutations at the central positions of the GGEEF sequence are detrimental to the functional activity of the enzyme. This DGC lacks the site for allosteric inhibition found in the other DGCs of Vibrio cholerae, suggesting a different mode of inhibitory control in this DGC
-
malfunction
-
inactivation of PA3177 renders Pseudomonas aeruginosa strain PAO1 biofilms susceptible to tobramycin and hydrogen peroxide. Inactivation of PA3177 also eliminates the recalcitrance of biofilms to killing by tobramycin, with multicopy expression of PA3177 but not PA3177_GGAAF harboring substitutions in the active site, restoring tolerance to wild-type levels. While PA3177 contributes to biofilm drug tolerance, inactivation of PA3177 has no effect on attachment and biofilm formation. Inactivation of PA3177 correlates with reduced c-di-GMP levels in biofilm but not planktonic cells. Inactivation of PA3177 has no effect on attachment and the formation of mature biofilms characterized by a three-dimensional biofilm architecture
-
malfunction
-
overexpression of SadC in Pseudomonas aeruginosa strain PAO1 totally inhibits swimming motility and significantly enhances the production of exopolysaccharide Psl. SadC lacking transmembrane domains (SadC300-487) cannot localize on cytoplasmic membrane and form cluster, loses the ability to inhibit the swimming and twitching motility, and shows the attenuated activity to promote Psl production despite that SadC300-487 is able to catalyze the synthesize of c-di-GMP in vitro and in vivo. Truncated enzyme version SadC300-487 can catalyze the synthesis of c-di-GMP in vitro, but version SadC323-487 cannot, structure-function analysis, overview
-
malfunction
-
weak product feedback inhibition is found in PA0847 GGDEF domain suggesting that allosteric regulation from the sensory domain could play a dominant role in the control of intracellular c-di-GMP synthesis
-
malfunction
-
enzyme inhibition by inhibitors causes inhibition of biofilm formation of the organism
-
malfunction
-
enzyme inhibition by inhibitors causes inhibition of biofilm formation of the organism
-
malfunction
-
inactivation of PA3177 renders Pseudomonas aeruginosa strain PAO1 biofilms susceptible to tobramycin and hydrogen peroxide. Inactivation of PA3177 also eliminates the recalcitrance of biofilms to killing by tobramycin, with multicopy expression of PA3177 but not PA3177_GGAAF harboring substitutions in the active site, restoring tolerance to wild-type levels. While PA3177 contributes to biofilm drug tolerance, inactivation of PA3177 has no effect on attachment and biofilm formation. Inactivation of PA3177 correlates with reduced c-di-GMP levels in biofilm but not planktonic cells. Inactivation of PA3177 has no effect on attachment and the formation of mature biofilms characterized by a three-dimensional biofilm architecture
-
malfunction
-
overexpression of SadC in Pseudomonas aeruginosa strain PAO1 totally inhibits swimming motility and significantly enhances the production of exopolysaccharide Psl. SadC lacking transmembrane domains (SadC300-487) cannot localize on cytoplasmic membrane and form cluster, loses the ability to inhibit the swimming and twitching motility, and shows the attenuated activity to promote Psl production despite that SadC300-487 is able to catalyze the synthesize of c-di-GMP in vitro and in vivo. Truncated enzyme version SadC300-487 can catalyze the synthesis of c-di-GMP in vitro, but version SadC323-487 cannot, structure-function analysis, overview
-
malfunction
-
weak product feedback inhibition is found in PA0847 GGDEF domain suggesting that allosteric regulation from the sensory domain could play a dominant role in the control of intracellular c-di-GMP synthesis
-
malfunction
-
enzyme inhibition by inhibitors causes inhibition of biofilm formation of the organism
-
malfunction
-
mutation in the GGDEF motif (from GGDEF to GGAAF) abolishes the c-di-GMP synthesis ability of GcsA
-
malfunction
-
mutation in the GGDEF motif (from GGDEF to GGAAF) abolishes the c-di-GMP synthesis ability of GcsA
-
malfunction
-
mutation in the GGDEF motif (from GGDEF to GGAAF) abolishes the c-di-GMP synthesis ability of GcsA
-
malfunction
-
the CdgD deletion mutant shows significant alteration in the biofilm formation compared to wild-type. Deletion of cdgD causes an increase in motility
-
malfunction
-
enzyme inhibition by inhibitors causes inhibition of biofilm formation of the organism
-
malfunction
-
the CdgD deletion mutant shows significant alteration in the biofilm formation compared to wild-type. Deletion of cdgD causes an increase in motility
-
malfunction
-
enzyme inhibition by inhibitors causes inhibition of biofilm formation of the organism
-
malfunction
-
inactivation of PA3177 renders Pseudomonas aeruginosa strain PAO1 biofilms susceptible to tobramycin and hydrogen peroxide. Inactivation of PA3177 also eliminates the recalcitrance of biofilms to killing by tobramycin, with multicopy expression of PA3177 but not PA3177_GGAAF harboring substitutions in the active site, restoring tolerance to wild-type levels. While PA3177 contributes to biofilm drug tolerance, inactivation of PA3177 has no effect on attachment and biofilm formation. Inactivation of PA3177 correlates with reduced c-di-GMP levels in biofilm but not planktonic cells. Inactivation of PA3177 has no effect on attachment and the formation of mature biofilms characterized by a three-dimensional biofilm architecture
-
malfunction
-
overexpression of SadC in Pseudomonas aeruginosa strain PAO1 totally inhibits swimming motility and significantly enhances the production of exopolysaccharide Psl. SadC lacking transmembrane domains (SadC300-487) cannot localize on cytoplasmic membrane and form cluster, loses the ability to inhibit the swimming and twitching motility, and shows the attenuated activity to promote Psl production despite that SadC300-487 is able to catalyze the synthesize of c-di-GMP in vitro and in vivo. Truncated enzyme version SadC300-487 can catalyze the synthesis of c-di-GMP in vitro, but version SadC323-487 cannot, structure-function analysis, overview
-
malfunction
-
weak product feedback inhibition is found in PA0847 GGDEF domain suggesting that allosteric regulation from the sensory domain could play a dominant role in the control of intracellular c-di-GMP synthesis
-
malfunction
-
enzyme inhibition by inhibitors causes inhibition of biofilm formation of the organism
-
malfunction
-
inactivation of PA3177 renders Pseudomonas aeruginosa strain PAO1 biofilms susceptible to tobramycin and hydrogen peroxide. Inactivation of PA3177 also eliminates the recalcitrance of biofilms to killing by tobramycin, with multicopy expression of PA3177 but not PA3177_GGAAF harboring substitutions in the active site, restoring tolerance to wild-type levels. While PA3177 contributes to biofilm drug tolerance, inactivation of PA3177 has no effect on attachment and biofilm formation. Inactivation of PA3177 correlates with reduced c-di-GMP levels in biofilm but not planktonic cells. Inactivation of PA3177 has no effect on attachment and the formation of mature biofilms characterized by a three-dimensional biofilm architecture
-
malfunction
-
overexpression of SadC in Pseudomonas aeruginosa strain PAO1 totally inhibits swimming motility and significantly enhances the production of exopolysaccharide Psl. SadC lacking transmembrane domains (SadC300-487) cannot localize on cytoplasmic membrane and form cluster, loses the ability to inhibit the swimming and twitching motility, and shows the attenuated activity to promote Psl production despite that SadC300-487 is able to catalyze the synthesize of c-di-GMP in vitro and in vivo. Truncated enzyme version SadC300-487 can catalyze the synthesis of c-di-GMP in vitro, but version SadC323-487 cannot, structure-function analysis, overview
-
malfunction
-
weak product feedback inhibition is found in PA0847 GGDEF domain suggesting that allosteric regulation from the sensory domain could play a dominant role in the control of intracellular c-di-GMP synthesis
-
malfunction
-
enzyme inhibition by inhibitors causes inhibition of biofilm formation of the organism
-
malfunction
-
inactivation of PA3177 renders Pseudomonas aeruginosa strain PAO1 biofilms susceptible to tobramycin and hydrogen peroxide. Inactivation of PA3177 also eliminates the recalcitrance of biofilms to killing by tobramycin, with multicopy expression of PA3177 but not PA3177_GGAAF harboring substitutions in the active site, restoring tolerance to wild-type levels. While PA3177 contributes to biofilm drug tolerance, inactivation of PA3177 has no effect on attachment and biofilm formation. Inactivation of PA3177 correlates with reduced c-di-GMP levels in biofilm but not planktonic cells. Inactivation of PA3177 has no effect on attachment and the formation of mature biofilms characterized by a three-dimensional biofilm architecture
-
malfunction
-
overexpression of SadC in Pseudomonas aeruginosa strain PAO1 totally inhibits swimming motility and significantly enhances the production of exopolysaccharide Psl. SadC lacking transmembrane domains (SadC300-487) cannot localize on cytoplasmic membrane and form cluster, loses the ability to inhibit the swimming and twitching motility, and shows the attenuated activity to promote Psl production despite that SadC300-487 is able to catalyze the synthesize of c-di-GMP in vitro and in vivo. Truncated enzyme version SadC300-487 can catalyze the synthesis of c-di-GMP in vitro, but version SadC323-487 cannot, structure-function analysis, overview
-
malfunction
-
weak product feedback inhibition is found in PA0847 GGDEF domain suggesting that allosteric regulation from the sensory domain could play a dominant role in the control of intracellular c-di-GMP synthesis
-
malfunction
-
enzyme inhibition by inhibitors causes inhibition of biofilm formation of the organism
-
malfunction
-
inactivation of PA3177 renders Pseudomonas aeruginosa strain PAO1 biofilms susceptible to tobramycin and hydrogen peroxide. Inactivation of PA3177 also eliminates the recalcitrance of biofilms to killing by tobramycin, with multicopy expression of PA3177 but not PA3177_GGAAF harboring substitutions in the active site, restoring tolerance to wild-type levels. While PA3177 contributes to biofilm drug tolerance, inactivation of PA3177 has no effect on attachment and biofilm formation. Inactivation of PA3177 correlates with reduced c-di-GMP levels in biofilm but not planktonic cells. Inactivation of PA3177 has no effect on attachment and the formation of mature biofilms characterized by a three-dimensional biofilm architecture
-
malfunction
-
overexpression of SadC in Pseudomonas aeruginosa strain PAO1 totally inhibits swimming motility and significantly enhances the production of exopolysaccharide Psl. SadC lacking transmembrane domains (SadC300-487) cannot localize on cytoplasmic membrane and form cluster, loses the ability to inhibit the swimming and twitching motility, and shows the attenuated activity to promote Psl production despite that SadC300-487 is able to catalyze the synthesize of c-di-GMP in vitro and in vivo. Truncated enzyme version SadC300-487 can catalyze the synthesis of c-di-GMP in vitro, but version SadC323-487 cannot, structure-function analysis, overview
-
malfunction
-
weak product feedback inhibition is found in PA0847 GGDEF domain suggesting that allosteric regulation from the sensory domain could play a dominant role in the control of intracellular c-di-GMP synthesis
-
malfunction
-
enzyme inhibition by inhibitors causes inhibition of biofilm formation of the organism
-
malfunction
-
inactivation of PA3177 renders Pseudomonas aeruginosa strain PAO1 biofilms susceptible to tobramycin and hydrogen peroxide. Inactivation of PA3177 also eliminates the recalcitrance of biofilms to killing by tobramycin, with multicopy expression of PA3177 but not PA3177_GGAAF harboring substitutions in the active site, restoring tolerance to wild-type levels. While PA3177 contributes to biofilm drug tolerance, inactivation of PA3177 has no effect on attachment and biofilm formation. Inactivation of PA3177 correlates with reduced c-di-GMP levels in biofilm but not planktonic cells. Inactivation of PA3177 has no effect on attachment and the formation of mature biofilms characterized by a three-dimensional biofilm architecture
-
malfunction
-
overexpression of SadC in Pseudomonas aeruginosa strain PAO1 totally inhibits swimming motility and significantly enhances the production of exopolysaccharide Psl. SadC lacking transmembrane domains (SadC300-487) cannot localize on cytoplasmic membrane and form cluster, loses the ability to inhibit the swimming and twitching motility, and shows the attenuated activity to promote Psl production despite that SadC300-487 is able to catalyze the synthesize of c-di-GMP in vitro and in vivo. Truncated enzyme version SadC300-487 can catalyze the synthesis of c-di-GMP in vitro, but version SadC323-487 cannot, structure-function analysis, overview
-
malfunction
-
weak product feedback inhibition is found in PA0847 GGDEF domain suggesting that allosteric regulation from the sensory domain could play a dominant role in the control of intracellular c-di-GMP synthesis
-
malfunction
-
enzyme inhibition by inhibitors causes inhibition of biofilm formation of the organism
-
malfunction
-
mutations at the central positions of the GGEEF sequence are detrimental to the functional activity of the enzyme. This DGC lacks the site for allosteric inhibition found in the other DGCs of Vibrio cholerae, suggesting a different mode of inhibitory control in this DGC
-
malfunction
-
mutations at the central positions of the GGEEF sequence are detrimental to the functional activity of the enzyme. This DGC lacks the site for allosteric inhibition found in the other DGCs of Vibrio cholerae, suggesting a different mode of inhibitory control in this DGC
-
malfunction
-
enzyme inhibition by inhibitors causes inhibition of biofilm formation of the organism
-
malfunction
-
enzyme inhibition by inhibitors causes inhibition of biofilm formation of the organism
-
malfunction
-
BpeGReg266 (residues 1-266) and BpeGReg296 (residues 1-296), which only contain the globin and middle domains, can inhibit bacterial motility. The distal residues of the globin domain affect diguanylate cyclase activity, Bpe-GReg may interact with other c-di-GMP-metabolizing proteins to form mixed signaling teams
-
malfunction
Pseudomonas fluorescens Pfl01
-
mutation of residues at the I-site of a DGC disrupts the interaction with its target receptor. By creating various substitutions to a DGC's I-site, it is shown that signaling between a DGC (GcbC) and its target protein (LapD) is a combined function of the I-site-dependent protein-protein interaction and the level of c-di-GMP production. Disruption of the I-site of GcbC leads to deregulation of c-di-GMP production, an increase in the c-di-GMP level and a concomitant increase in c-di-GMP-regulated processes
-
malfunction
-
BpeGReg266 (residues 1-266) and BpeGReg296 (residues 1-296), which only contain the globin and middle domains, can inhibit bacterial motility. The distal residues of the globin domain affect diguanylate cyclase activity, Bpe-GReg may interact with other c-di-GMP-metabolizing proteins to form mixed signaling teams
-
metabolism
-
propose of a pathway consisting of GcpA-H-NS-RsmB-RsmA-pelD, that controls Pel production in Dickeya dadantii, overview. Of the two PDEs involved in the regulation of Pels, only EGcpB regulates pelD expression through the same pathway as GcpA. GcpA regulates Pel through the Rsm system, H-NS is involved in the GcpA-Rsm pathway. H-NS and Rsm play different roles in the GcpAdependent regulation of swimming motility and T3SS, H-NS is not involved in the regulation of T3SS in either the Dickeya dadantii wild-type or gcpAD418A strain
metabolism
the HptB pathway controls biofilm formation, swarming motility by involving both HsbD and the anti-anti-sigma factor HsbA. The rewiring of c-di-GMP signaling into the HptB cascade relies on the original interaction between HsbD and HsbA and on the control of HsbD dynamic localization at the cell poles. The hptB gene cluster merges with flagellar and chemotaxis genes to evolve into a distinct Pseudomonas aeruginosa-specific flagellar locus. HsbD is a diguanylate cyclase which activity intersects with the HptB regulatory pathway. DGC enzymes SadC and HsbD differentially impact HptB-dependent phenotypes
metabolism
-
AdrA acts independently of the Gac system, which is also consistent with the activity of AdrA in the SadB branch of the signaling pathway, hypothetical regulatory model for flagellar synthesis in Pseudomonas fluorescens strain F113, overview
metabolism
cyclic diguanylate (c-di-GMP) is a near universal signaling molecule produced by diguanylate cyclases that can direct a variety of bacterial behaviors. Effectors, e.g. LapD, can sense the c-di-GMP signal from a specific DGC. Relationship between DGC-effector contact and catalysis. Dynamics of a signaling complex, distinguishing interaction versus signaling, and relationship between local and global signaling, overview. Modeling
metabolism
-
cyclic diguanylate (c-di-GMP) is a near universal signaling molecule produced by diguanylate cyclases that can direct a variety of bacterial behaviors. Effectors, e.g. LapD, can sense the c-di-GMP signal from a specific DGC. Relationship between DGC-effector contact and catalysis. Dynamics of a signaling complex, distinguishing interaction versus signaling, and relationship between local and global signaling, overview. Modeling
metabolism
-
cyclic diguanylate (c-di-GMP) is a near universal signaling molecule produced by diguanylate cyclases that can direct a variety of bacterial behaviors. Effectors, e.g. LapD, can sense the c-di-GMP signal from a specific DGC. Relationship between DGC-effector contact and catalysis. Dynamics of a signaling complex, distinguishing interaction versus signaling, and relationship between local and global signaling, overview. Modeling
metabolism
BrlR is a c-di-GMP responsive transcriptional regulator. Inactivation of PA3177 coincides with BrlR abundance being reduced in biofilms and unable to bind to PmexE, inactivation of PA3177 coincides with reduced BrlR protein abundance
metabolism
-
cyclic diguanylate (c-di-GMP) is a near universal signaling molecule produced by diguanylate cyclases that can direct a variety of bacterial behaviors. Effectors, e.g. LapD, can sense the c-di-GMP signal from a specific DGC. Relationship between DGC-effector contact and catalysis. Dynamics of a signaling complex, distinguishing interaction versus signaling, and relationship between local and global signaling, overview. Modeling
metabolism
-
cyclic diguanylate (c-di-GMP) is a near universal signaling molecule produced by diguanylate cyclases that can direct a variety of bacterial behaviors. Effectors, e.g. LapD, can sense the c-di-GMP signal from a specific DGC. Relationship between DGC-effector contact and catalysis. Dynamics of a signaling complex, distinguishing interaction versus signaling, and relationship between local and global signaling, overview. Modeling
metabolism
-
cyclic diguanylate (c-di-GMP) is a near universal signaling molecule produced by diguanylate cyclases that can direct a variety of bacterial behaviors. Effectors, e.g. LapD, can sense the c-di-GMP signal from a specific DGC. Relationship between DGC-effector contact and catalysis. Dynamics of a signaling complex, distinguishing interaction versus signaling, and relationship between local and global signaling, overview. Modeling
metabolism
cyclic diguanylate (c-di-GMP) is a near universal signaling molecule produced by diguanylate cyclases that can direct a variety of bacterial behaviors. Effectors, e.g. LapD, can sense the c-di-GMP signal from a specific DGC. Relationship between DGC-effector contact and catalysis. Dynamics of a signaling complex, distinguishing interaction versus signaling, and relationship between local and global signaling, overview. Modeling
metabolism
DGC SadC is more effective than DGC WspR in promoting Psl synthesis in Pseudomonas aeruginosa strain PAO1
metabolism
DgcZ shows interaction with FrdB, a subunit of the fumarate reductase complex (FRD) involved in anaerobic respiration and in control of flagellum assembly, determined by coimmunoprecipitation analysis and bacterial-two-hybrid assay. The FRD complex is required for the increase in DgcZ-mediated biofilm formation upon induction of oxidative stress by addition of paraquat
metabolism
-
propose of a pathway consisting of GcpA-H-NS-RsmB-RsmA-pelD, that controls Pel production in Dickeya dadantii, overview. Of the two PDEs involved in the regulation of Pels, only EGcpB regulates pelD expression through the same pathway as GcpA. GcpA regulates Pel through the Rsm system, H-NS is involved in the GcpA-Rsm pathway. H-NS and Rsm play different roles in the GcpAdependent regulation of swimming motility and T3SS, H-NS is not involved in the regulation of T3SS in either the Dickeya dadantii wild-type or gcpAD418A strain
-
metabolism
-
the HptB pathway controls biofilm formation, swarming motility by involving both HsbD and the anti-anti-sigma factor HsbA. The rewiring of c-di-GMP signaling into the HptB cascade relies on the original interaction between HsbD and HsbA and on the control of HsbD dynamic localization at the cell poles. The hptB gene cluster merges with flagellar and chemotaxis genes to evolve into a distinct Pseudomonas aeruginosa-specific flagellar locus. HsbD is a diguanylate cyclase which activity intersects with the HptB regulatory pathway. DGC enzymes SadC and HsbD differentially impact HptB-dependent phenotypes
-
metabolism
-
BrlR is a c-di-GMP responsive transcriptional regulator. Inactivation of PA3177 coincides with BrlR abundance being reduced in biofilms and unable to bind to PmexE, inactivation of PA3177 coincides with reduced BrlR protein abundance
-
metabolism
-
DGC SadC is more effective than DGC WspR in promoting Psl synthesis in Pseudomonas aeruginosa strain PAO1
-
metabolism
-
BrlR is a c-di-GMP responsive transcriptional regulator. Inactivation of PA3177 coincides with BrlR abundance being reduced in biofilms and unable to bind to PmexE, inactivation of PA3177 coincides with reduced BrlR protein abundance
-
metabolism
-
DGC SadC is more effective than DGC WspR in promoting Psl synthesis in Pseudomonas aeruginosa strain PAO1
-
metabolism
-
BrlR is a c-di-GMP responsive transcriptional regulator. Inactivation of PA3177 coincides with BrlR abundance being reduced in biofilms and unable to bind to PmexE, inactivation of PA3177 coincides with reduced BrlR protein abundance
-
metabolism
-
DGC SadC is more effective than DGC WspR in promoting Psl synthesis in Pseudomonas aeruginosa strain PAO1
-
metabolism
-
BrlR is a c-di-GMP responsive transcriptional regulator. Inactivation of PA3177 coincides with BrlR abundance being reduced in biofilms and unable to bind to PmexE, inactivation of PA3177 coincides with reduced BrlR protein abundance
-
metabolism
-
DGC SadC is more effective than DGC WspR in promoting Psl synthesis in Pseudomonas aeruginosa strain PAO1
-
metabolism
-
BrlR is a c-di-GMP responsive transcriptional regulator. Inactivation of PA3177 coincides with BrlR abundance being reduced in biofilms and unable to bind to PmexE, inactivation of PA3177 coincides with reduced BrlR protein abundance
-
metabolism
-
DGC SadC is more effective than DGC WspR in promoting Psl synthesis in Pseudomonas aeruginosa strain PAO1
-
metabolism
-
BrlR is a c-di-GMP responsive transcriptional regulator. Inactivation of PA3177 coincides with BrlR abundance being reduced in biofilms and unable to bind to PmexE, inactivation of PA3177 coincides with reduced BrlR protein abundance
-
metabolism
-
DGC SadC is more effective than DGC WspR in promoting Psl synthesis in Pseudomonas aeruginosa strain PAO1
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metabolism
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BrlR is a c-di-GMP responsive transcriptional regulator. Inactivation of PA3177 coincides with BrlR abundance being reduced in biofilms and unable to bind to PmexE, inactivation of PA3177 coincides with reduced BrlR protein abundance
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metabolism
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DGC SadC is more effective than DGC WspR in promoting Psl synthesis in Pseudomonas aeruginosa strain PAO1
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metabolism
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AdrA acts independently of the Gac system, which is also consistent with the activity of AdrA in the SadB branch of the signaling pathway, hypothetical regulatory model for flagellar synthesis in Pseudomonas fluorescens strain F113, overview
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metabolism
Vibrio cholerae serotype O1 A1552
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cyclic diguanylate (c-di-GMP) is a near universal signaling molecule produced by diguanylate cyclases that can direct a variety of bacterial behaviors. Effectors, e.g. LapD, can sense the c-di-GMP signal from a specific DGC. Relationship between DGC-effector contact and catalysis. Dynamics of a signaling complex, distinguishing interaction versus signaling, and relationship between local and global signaling, overview. Modeling
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physiological function
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in Gram-negative bacteria production of of cyclic di-3',5'-guanylate, c-di-GMP, is the main trigger for production of extracellular polysaccharides and for biofilm formation
physiological function
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SwDGC is capable of affecting extracellular polysaccharide matrix production, presumably by altering intracellular c-di-GMP levels
physiological function
the protein reversibly photoconverts between blue- and green-absorbing forms, and has diguanylate cyclase activity, which is enhanced 38fold by blue light compared with green light. The protein's relatively low affinity for Mg2+, which is essential for diguanylate cyclase activity, suggests thatMg2might also regulate cyclic-di-GMP signaling. Blue light irradiation under low temperature is responsible for Thermosynechococcus vulcanus cell aggregation, which is abolished when gene Tlr0924 is disrupted
physiological function
Q8PPS5
protein has in vivo and in vitro diguanylate cyclase activity that leads to the production of cyclic di-GMP. Protein XAC0610 plays a role in the regulation of Xanthomonas citri motility and resistance to H2O2. XAC0610 is not subject to allosteric product inhibition. Instead, steady-state kinetics reveal a positive cooperative effect of the GTP substrate with a dissociation constant for the binding of the first GTP molecule (K1) approximately 5 times greater than the dissociation constant for the binding of the second GTP molecule (K2). The N-terminal GAF and PAS domains are required for high levels of XAC0610 diguanylate cyclase activity
physiological function
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isoform Chp8 is a functional diguanylate cyclase expressed in response to plant signals and codependent enhancer-binding proteins HrpRS. Chp8 decreases the expression of the major pathogen-associated molecular pattern flagellin and increases extracellular polysaccharides and impacts the salicylic acid/jasmonic acid hormonal immune response and disease progression
physiological function
diguanylate cyclase YfiN acts as a bifunctional protein that produces cyclic di-GMP in response to reductive stress and then dynamically relocates to the division site to arrest cell division in response to envelope stress in Escherichia coli. YfiN localizes to the Z ring by interacting with early division proteins and stalls cell division by preventing the initiation of septal peptidoglycan synthesis
physiological function
ML1419c expression in Pseudomonas aeruginosa alters colony morphology, motility and biofilm formation in a manner consistent with increased cyclic di-GMP production. ML1419c expression increases cyclic di-GMP production in cultures in comparison to the vector control. The observed phenotypes and increased levels of cyclic di-GMP can be abrogated by mutation of the active site in ML1419c
physiological function
the cdgA gene encoding diguanylate cyclase A is involved in biofilm formation and exopolysaccharide production in Azospirillum brasilense. Bacteria harboring a cdgA mutation exhibit biofilms with considerably reduced thickness compared with those of the wild-type strain. Extracellular DNA and exopolysaccharide are components of the biofilm matrix in Azospirillum
physiological function
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DosD is a direct oxygen-sensing diguanylate cyclase playing a regulatory role in biofilm formation by Shewanella putrefaciens CN32 under aerobic conditions. The activity of DosD culminates to synthesis of cyclic diguanylate in the presence of oxygen. DosD regulates the transcription of the bpfA operon which encodes seven proteins including a large repetitive adhesin BpfA and its cognate type I secretion system (TISS). Regulation of DosD in aerobic biofilms is heavily dependent on an adhesin BpfA and the TISS
physiological function
DgcA negatively affects virulence, extracellular polymeric substances production, bacterial autoaggregation and motility, but positively triggers biofilm formation via modulating the intracellular cyclic di-GMP levels. Deletion of dgcA substantially increases Xoo virulence against two different rice cultivars. 349 differentially expressed genes are controlled by DgcA
physiological function
Dcsbis tightly coordinates cell motility without markedly affecting biofilm formation and is a diguanylate cyclase with a catalytic activity much higher than those of many other diguanylate cyclases
physiological function
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overexpression of either diguanylate cyclase genes, celR (atu1297) and atu1060 results in increased cellulose production, while deletion of celR, but not atu1060, results in decreased cellulose biosynthesis. celR overexpression also affects biofilm formation, formation of a polar adhesion structure, plant surface attachment, and virulence, suggesting that the gene plays a role in regulating these processes
physiological function
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overexpression of either diguanylate cyclase genes, celR (atu1297) and atu1060 results in increased cellulose production, while deletion of celR, but not atu1060, results in decreased cellulose biosynthesis
physiological function
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ectopic expression of VCA0965 in ibrio. cholerae causes a 3fold reduction in flagellar-based motility. An RXXD allosteric inhibition mutant of VCA0965 strongly inhibits motility and stimulates biofilm formation. This activity is lost when the active site of VCA0965 is mutated to AGDAF, suggesting that VCA0965 synthesizes cyclic-di-GMP. Ectopic expression of VCA0965 and VCA0965 containing a mutation in its RXXD motif significantly increases the intracellular cyclic-di-GMP levels in Vibrio cholerae and Escherichia coli. Purified VCA0965 is able to synthesize cyclic-di-GMP in vitro
physiological function
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enzymic activity is dependent on the integrity of its GGDEF domain. Deletion of the dgcP gene shows that DgcP negatively regulates motility and positively controls biofilm formation, the deletion mutant mutant is hypovirulent in olive plants. Overexpression of the gene leads to an enhanced CR-binding phenotype that was accompanied by the formation of wrinkly colonies
physiological function
DgcP negatively regulates motility and positively controls biofilm formation. Overexpression of the DgcP gene leads to increased exopolysaccharide production and upregulation of the type VI secretion system, in turn, it represses the type III secretion system, a hallmark of chronic infections and persistence for P.seudomonasaeruginosa. Deletion of the DgcP gene reduces the virulence in a mouse acute lung injury model
physiological function
a deletion mutation in the pgn_1932 gene has a significant effect on the intracellular cyclic-di-GMP level in Porphyromonas gingivalis. Expression of the fimA and rgpA genes, encoding the major protein subunit of fimbriae and an arginine-specific proteinase, respectively, is downregulated in the pgn_1932 mutant. Correspondingly, FimA protein production and the fimbrial display on the mutant are significantly reduced. Mutations in the pgn_1932 gene also have a significant impact on the adhesive and invasive capabilities of P.orphyromonas gingivalis, which are required for its pathogenicity
physiological function
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enzyme synthesizes cyclic-di-GMP to regulate surface attachment via modulation of motility, without affecting subsequent biofilm formation. GcbA regulates flagellum-driven motility by suppressing flagellar reversal rates in a manner independent of viscosity, surface hardness, and polysaccharide production
physiological function
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Pseudomonas fluorescens GcbA is functional in P.seudomonas aeruginosa and is capable of restoring phenotypes associated with inactivation of gcbA in P.seudomonas aeruginosa to wild-type levels. Motility and attachment of a gcbA mutant strain can be restored to wild-type levels via overexpression of the small regulatory RNA RsmZ. While both contribute to the regulation of initial surface attachment and flagellum-driven motility, GcbA and the phosphodiesterase DipA act within different signaling networks to regulate these processes
physiological function
the primary signaling molecule promoting bacterial biofilm formation is the universal second messenger cyclic di-GMP. This dinucleotide predominantly controls the gene expression of motility, adhesins, and capsule production to coordinate biofilm formation. Cyclic di-GMP is synthesized by diguanylate cyclases (DGCs) that have a GGDEF domain and is degraded by phosphodiesterases (PDEs) containing either an EAL or an HD-GYP domain
physiological function
globin-coupled oxygen sensor with diguanylate cyclase activity from Escherichia coli, regulates cyclic-di-GMP synthesis based on oxygen availability. Cyclic-di-guanosine-5'-monophosphate (c-di-GMP) is an important bacterial second messenger that regulates many key physiological functions including cell motility, differentiation, development, virulence, biofilm formation, cell-cell communication, and environmental persistence
physiological function
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the diguanylate cyclase GcpA inhibits the production of pectate lyases (Pel) via the H-NS protein and RsmB regulatory RNA in Dickeya dadantii. GcpA is the dominant DGC to negatively regulate Pel production by the specific repression of pelD gene expression. The DGC activity of GcpA is essential for its regulation of Pel production. Quantitative reverse transcription-polymerase chain reaction (qRT-PCR) assays reveal that the expression levels of histone-like, nucleoid-structuring protein encoding gene hns and posttranscriptional regulator encoding genes rsmA and rsmB are significantly affected by GcpA. H-NS and RsmB are responsible for the GcpA-dependent regulation of motility and type III secretion system (T3SS) gene expression, respectively. Gene gcpA might be essential for the viability of Dickeya dadantii, a functional A-site is required for GGDEF domain activity. GcpA negatively regulates the virulence, swimming motility, and T3SS gene expression of Dickeya dadantii
physiological function
the intracellular concentration of c-di-GMP determines both bacterial physiology and pathogenesis. HsbD is a diguanylate cyclase which activity intersects with the HptB regulatory pathway. The enzyme synthesizes c-di-GMP to locally implement the HptB regulatory pathway for the control of swarming, twitching, swimming motilities and biofilmformation. The HptB pathway controls biofilm formation and motility by involving both HsbD and the anti-anti-sigma factor HsbA. HsbD modulates type IV pili assembly and twitching motility and impacts swarming motility, overview. The rewiring of c-di-GMP signaling into the HptB cascade relies on the original interaction between HsbD and HsbA and on the control of HsbD dynamic localization at the cell poles
physiological function
-
diguanylate cyclases (DGCs) are responsible for the synthesis of second messenger cyclic di-guanosine monophosphate (c-di-GMP), which are involved in various physiological activities of bacterial species. DGC catalyzes the reaction of cyclic di-guanosine monophosphate (c-di-GMP) synthesis using guanosine triphosphate (GTP) as substrate. c-di-GMP is one of the potent regulator molecules, which is involved in many bacterial cellular functions, such as virulence, motility, bioluminescence, cellulose biosynthesis, adhesion, secretion, community behavior, biofilm formation, and cell differentiation
physiological function
3',5'-cyclic diguanylate monophosphate (c-di-GMP) is a ubiquitous secondary messenger that plays a key role in response regulation and lifestyle conventions of pathogenic bacteria, including Vibrio cholerae. Increases in c-di-GMP levels induce increased expression of various factors necessary for the establishment and maintenance of biofilm communities, whereas decreased levels usually lead to enhanced expression of virulence and motility factors related to biofilm degradation. C-di-GMP is synthesized from guanosine triphosphate by diguanylate cyclase (DGC) enzymes
physiological function
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the diguanylate cyclase AdrA regulates flagellar biosynthesis in Pseudomonas fluorescens F113 through SadB. AdrA is a diguanylate cyclase implicated in c-di-GMP-mediated cellulose production and biofilm formation. AdrA is involved in swimming and biofilm formation, since inactivation of the adrA gene results in increased swimming motility and a reduction in the initial stages of attachment to surfaces. The enzyme is implicated in flagellar gene expression, genetic interaction between adrA and sadB indicates that AdrA participates in the regulation of flagella biogenesis
physiological function
GcsA inhibits swimming motility in an FlgZ-dependent manner. The GGDEF domain of GcsA contains all the conserved signature amino acid residues that form the enzyme's active site, as well as other residues required for the diguanylate cyclase activity of the GGDEF domain. GcsA modulates the cellular cyclic di-GMP level at early exponential phase
physiological function
PA3177 is confirmed to be an active diguanylate cyclase, with overexpression affecting swimming and swarming motility, and inactivation affecting cellular bis-(3'-5')-cyclic dimeric GMP (c-di-GMP) levels of biofilm but not planktonic cells. PA3177 is confirmed to be an active diguanylate cyclase, with overexpression affecting swimming and swarming motility, and inactivation affecting cellular c-di-GMP levels of biofilm but not planktonic cells. While PA3177 contributes to biofilm drug tolerance, inactivation of PA3177 has no effect on attachment and biofilm formation
physiological function
cyclic diguanosine monophosphate (c-di-GMP) is one of the most important bacterial second messengers that controls many bacterial cellular functions including lifestyle switch between plankton and biofilm. Surface attachment defective (SadC) is a diguanylate cyclase (DGC) involved in the biosynthesis of c-di-GMP in Pseudomonas aeruginosa. SadC is reported to contribute to sensing of Psl and correspondingly increase of cellular c-di-GMP level. Involvement of Psl signalling in the SadC-mediated c-di-GMP synthesis
physiological function
the enzyme synthesizes the central signaling molecule, cyclic diguanylate (c-di-GMP), which is found to regulate various bacterial phenotypes, especially those involved in pathogen infection and drug resistance. Enzyme PA0847 is an active diguanylate cyclase (DGC). Roles of PA0847 in the regulation of bacterial motility and biofilm formation. Enzyme PA0847 is involved in response to a variety of environmental nutrients and factors, suggesting it might serve as a broad-range environmental sensor on the membrane of Pseudomonas aeruginosa. Gene of PA0847 affects biofilm formation and motility phenotypes in Pseudomonas aeruginosa
physiological function
Escherichia coli diguanylate cyclase DgcZ interlinks surface sensing and adhesion via multiple regulatory routes. A FRD complex is required for the increase in DgcZ-mediated biofilm formation upon induction of oxidative stress by addition of paraquat. Possible integrative role of DgcZ in regulation of surface attachment. Both DgcZ-stimulated PGA biosynthesis and interaction of DgcZ with the FRD complex contribute to impeding bacterial escape from the surface. DgcZ is the main DGC involved in PGA production in Escherichia coli. Abundance and activity of DgcZ are regulated at several levels. Gene dgcZ transcription is activated by the transcriptional regulator CpxR. Beyond transcriptional and translational regulation of protein concentration, DgcZ activity is regulated by Zn2+. DgcZ localization and c-di-GMP concentrations change between transition and stationary phase
physiological function
many bacteria contain large cyclic diguanylate (c-di-GMP) signaling networks made of diguanylate cyclases (DGCs) and phosphodiesterases that can direct cellular activities sensitive to c-di-GMP levels. While DGCs synthesize c-di-GMP, many DGCs also contain an autoinhibitory site (I-site) that binds c-di-GMP to halt excess production of this small molecule, thus controlling the amount of c-di-GMP available to bind to target proteins in the cell. Signaling between a DGC (GcbC) and its target protein (LapD) is a combined function of the I-site-dependent protein-protein interaction and the level of c-di-GMP production. The dual role of the I-site in modulating DGC activity as well as participating in protein-protein interactions suggests caution in interpreting the function of the I-site as only a means to negatively regulate a cyclase. These results implicate the I-site as an important positive and negative regulatory element of DGCs that may contribute to signaling specificity. Signaling specificity in Pseudomonas fluorescens is achieved by physical interaction is the regulation of biofilm formation by the inner membrane proteins GcbC and LapD. GcbC is a DGC that signals to the effector LapD. When bound to c-di-GMP, LapD changes conformation to sequester a periplasmic protease called LapG, thus allowing the large adhesin LapA to accumulate on the cell surface and thereby promoting biofilm formation
physiological function
enzyme Lcd1 is a potential node for the integration of cAMP and c-di-GMP signaling in Leptospira interrogans
physiological function
the second messenger cyclic dimeric guanosine monophosphate (c-di-GMP) is ubiquitous in bacteria. It is synthesized from two molecules of GTP by diguanylate cyclases (DGCs), which possess the c-di-GMP synthesis GGDEF domain. In the unicellular cyanobacterium Synechocystis sp. PCC 6803 (Synechocystis) c-di-GMP influences the decision between motility and sessility. The photoreceptor Cph2 from the cyanobacterium Synechocystis sp. PCC 6803 comprises three domains related to c-di-GMP metabolism: two GGDEF and one EAL domain. It has been shown that the C-terminal GGDEF domain acts as blue-light triggered c-di-GMP producer thereby inhibiting motility of the cells in blue light. Binding of Cph2 and Slr1143 is likely mediated through interaction of Cph2 with the GGDEF domain of Slr1143, the interaction is not stoichiometric. Analysis of protein-protein interaction of Slr1143 with Cph2, overview
physiological function
the primary signaling molecule promoting bacterial biofilm formation is the universal second messenger cyclic di-GMP. This dinucleotide predominantly controls the gene expression of motility, adhesins, and capsule production to coordinate biofilm formation. Cyclic di-GMP is synthesized by diguanylate cyclases (DGCs) that have a GGDEF domain and is degraded by phosphodiesterases (PDEs) containing either an EAL or an HD-GYP domain. The enzyme is important for the organism's biofilm formation ability, which plays a pivotal role in the virulence
physiological function
-
diguanylate cyclases in Vibrio cholerae are essential regulators of lifestyle switching, importance of DGCs and their product, cyclic-di-GMP, in the virulence and lifecycle of the bacteria. Biofilm formation in Vibrio cholerae empowers the bacteria to lead a dual lifestyle and enhances its infectivity. While the formation and dispersal of the biofilm involves multiple components, both proteinaceous and non-proteinaceous, the key to the regulatory control lies with the ubiquitous secondary signaling molecule, cyclic-di-GMP (c-di-GMP). Enzyme CdgH has a GGDEF domain along with a sensory PAS domain. It is a diguanylate cyclase. CdgH positively regulats the rugosity of the cel
physiological function
diguanylate cyclases in Vibrio cholerae are essential regulators of lifestyle switching, importance of DGCs and their product, cyclic-di-GMP, in the virulence and lifecycle of the bacteria. Biofilm formation in Vibrio cholerae empowers the bacteria to lead a dual lifestyle and enhances its infectivity. While the formation and dispersal of the biofilm involves multiple components, both proteinaceous and non-proteinaceous, the key to the regulatory control lies with the ubiquitous secondary signaling molecule, cyclic-di-GMP (c-di-GMP). Enzyme CdgD has a GGDEF domain along with a sensory PAS domain. It is a diguanylate cyclase. The enzyme does not have the conserved GGDEF motif, but has a degenerate AGDEF site. Significantly, expression of VCA0965 in Vibrio cholerae causes a 3fold reduction in flagellar-based motility. But enzyme VCA0965, despite its degenerate active site, synthesizes c-di-GMP
physiological function
diguanylate cyclases in Vibrio cholerae are essential regulators of lifestyle switching, importance of DGCs and their product, cyclic-di-GMP, in the virulence and lifecycle of the bacteria. Biofilm formation in Vibrio cholerae empowers the bacteria to lead a dual lifestyle and enhances its infectivity. While the formation and dispersal of the biofilm involves multiple components, both proteinaceous and non-proteinaceous, the key to the regulatory control lies with the ubiquitous secondary signaling molecule, cyclic-di-GMP (c-di-GMP). Enzyme VC0395_0300 is a diguanylate cyclase with a GGEEF domain, it synthesizes c-di-GMP actively and has an essential role to play in the biofilm formation of Vibrio cholerae
physiological function
diguanylate cyclase (DGC) synthesizes the ubiquitous bacterial second messenger c-di-GMP. GcsA has no PDE activity. GcsA modulates the cellular c-di-GMP level at early exponential phase. Crosstalk between c-di-GMP and cAMP in the regulation of the expression of GcsA in Pseudomonas putida. GcsA plays a role in early biofilm formation of Pseudomonas putida and regulates the swimming motility in an FlgZ-dependent manner
physiological function
A0A170Y3L9
the primary signaling molecule promoting bacterial biofilm formation is the universal second messenger cyclic di-GMP. This dinucleotide predominantly controls the gene expression of motility, adhesins, and capsule production to coordinate biofilm formation. Cyclic di-GMP is synthesized by diguanylate cyclases (DGCs) that have a GGDEF domain and is degraded by phosphodiesterases (PDEs) containing either an EAL or an HD-GYP domain. The enzyme is important for the organism's biofilm formation ability, which plays a pivotal role in the virulence
physiological function
the primary signaling molecule promoting bacterial biofilm formation is the universal second messenger cyclic di-GMP. This dinucleotide predominantly controls the gene expression of motility, adhesins, and capsule production to coordinate biofilm formation. Cyclic di-GMP is synthesized by diguanylate cyclases (DGCs) that have a GGDEF domain and is degraded by phosphodiesterases (PDEs) containing either an EAL or an HD-GYP domain. The enzyme is important for the organism's biofilm formation ability, which plays a pivotal role in the virulence
physiological function
the primary signaling molecule promoting bacterial biofilm formation is the universal second messenger cyclic di-GMP. This dinucleotide predominantly controls the gene expression of motility, adhesins, and capsule production to coordinate biofilm formation. Cyclic di-GMP is synthesized by diguanylate cyclases (DGCs) that have a GGDEF domain and is degraded by phosphodiesterases (PDEs) containing either an EAL or an HD-GYP domain
physiological function
the primary signaling molecule promoting bacterial biofilm formation is the universal second messenger cyclic di-GMP. This dinucleotide predominantly controls the gene expression of motility, adhesins, and capsule production to coordinate biofilm formation. Cyclic di-GMP is synthesized by diguanylate cyclases (DGCs) that have a GGDEF domain and is degraded by phosphodiesterases (PDEs) containing either an EAL or an HD-GYP domain
physiological function
the primary signaling molecule promoting bacterial biofilm formation is the universal second messenger cyclic di-GMP. This dinucleotide predominantly controls the gene expression of motility, adhesins, and capsule production to coordinate biofilm formation. Cyclic di-GMP is synthesized by diguanylate cyclases (DGCs) that have a GGDEF domain and is degraded by phosphodiesterases (PDEs) containing either an EAL or an HD-GYP domain
physiological function
the primary signaling molecule promoting bacterial biofilm formation is the universal second messenger cyclic di-GMP. This dinucleotide predominantly controls the gene expression of motility, adhesins, and capsule production to coordinate biofilm formation. Cyclic di-GMP is synthesized by diguanylate cyclases (DGCs) that have a GGDEF domain and is degraded by phosphodiesterases (PDEs) containing either an EAL or an HD-GYP domain
physiological function
-
isoform Chp8 is a functional diguanylate cyclase expressed in response to plant signals and codependent enhancer-binding proteins HrpRS. Chp8 decreases the expression of the major pathogen-associated molecular pattern flagellin and increases extracellular polysaccharides and impacts the salicylic acid/jasmonic acid hormonal immune response and disease progression
-
physiological function
-
the cdgA gene encoding diguanylate cyclase A is involved in biofilm formation and exopolysaccharide production in Azospirillum brasilense. Bacteria harboring a cdgA mutation exhibit biofilms with considerably reduced thickness compared with those of the wild-type strain. Extracellular DNA and exopolysaccharide are components of the biofilm matrix in Azospirillum
-
physiological function
-
the primary signaling molecule promoting bacterial biofilm formation is the universal second messenger cyclic di-GMP. This dinucleotide predominantly controls the gene expression of motility, adhesins, and capsule production to coordinate biofilm formation. Cyclic di-GMP is synthesized by diguanylate cyclases (DGCs) that have a GGDEF domain and is degraded by phosphodiesterases (PDEs) containing either an EAL or an HD-GYP domain
-
physiological function
-
DgcP negatively regulates motility and positively controls biofilm formation. Overexpression of the DgcP gene leads to increased exopolysaccharide production and upregulation of the type VI secretion system, in turn, it represses the type III secretion system, a hallmark of chronic infections and persistence for P.seudomonasaeruginosa. Deletion of the DgcP gene reduces the virulence in a mouse acute lung injury model
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physiological function
-
the diguanylate cyclase GcpA inhibits the production of pectate lyases (Pel) via the H-NS protein and RsmB regulatory RNA in Dickeya dadantii. GcpA is the dominant DGC to negatively regulate Pel production by the specific repression of pelD gene expression. The DGC activity of GcpA is essential for its regulation of Pel production. Quantitative reverse transcription-polymerase chain reaction (qRT-PCR) assays reveal that the expression levels of histone-like, nucleoid-structuring protein encoding gene hns and posttranscriptional regulator encoding genes rsmA and rsmB are significantly affected by GcpA. H-NS and RsmB are responsible for the GcpA-dependent regulation of motility and type III secretion system (T3SS) gene expression, respectively. Gene gcpA might be essential for the viability of Dickeya dadantii, a functional A-site is required for GGDEF domain activity. GcpA negatively regulates the virulence, swimming motility, and T3SS gene expression of Dickeya dadantii
-
physiological function
-
diguanylate cyclases in Vibrio cholerae are essential regulators of lifestyle switching, importance of DGCs and their product, cyclic-di-GMP, in the virulence and lifecycle of the bacteria. Biofilm formation in Vibrio cholerae empowers the bacteria to lead a dual lifestyle and enhances its infectivity. While the formation and dispersal of the biofilm involves multiple components, both proteinaceous and non-proteinaceous, the key to the regulatory control lies with the ubiquitous secondary signaling molecule, cyclic-di-GMP (c-di-GMP). Enzyme VC0395_0300 is a diguanylate cyclase with a GGEEF domain, it synthesizes c-di-GMP actively and has an essential role to play in the biofilm formation of Vibrio cholerae
-
physiological function
-
the intracellular concentration of c-di-GMP determines both bacterial physiology and pathogenesis. HsbD is a diguanylate cyclase which activity intersects with the HptB regulatory pathway. The enzyme synthesizes c-di-GMP to locally implement the HptB regulatory pathway for the control of swarming, twitching, swimming motilities and biofilmformation. The HptB pathway controls biofilm formation and motility by involving both HsbD and the anti-anti-sigma factor HsbA. HsbD modulates type IV pili assembly and twitching motility and impacts swarming motility, overview. The rewiring of c-di-GMP signaling into the HptB cascade relies on the original interaction between HsbD and HsbA and on the control of HsbD dynamic localization at the cell poles
-
physiological function
-
PA3177 is confirmed to be an active diguanylate cyclase, with overexpression affecting swimming and swarming motility, and inactivation affecting cellular bis-(3'-5')-cyclic dimeric GMP (c-di-GMP) levels of biofilm but not planktonic cells. PA3177 is confirmed to be an active diguanylate cyclase, with overexpression affecting swimming and swarming motility, and inactivation affecting cellular c-di-GMP levels of biofilm but not planktonic cells. While PA3177 contributes to biofilm drug tolerance, inactivation of PA3177 has no effect on attachment and biofilm formation
-
physiological function
-
cyclic diguanosine monophosphate (c-di-GMP) is one of the most important bacterial second messengers that controls many bacterial cellular functions including lifestyle switch between plankton and biofilm. Surface attachment defective (SadC) is a diguanylate cyclase (DGC) involved in the biosynthesis of c-di-GMP in Pseudomonas aeruginosa. SadC is reported to contribute to sensing of Psl and correspondingly increase of cellular c-di-GMP level. Involvement of Psl signalling in the SadC-mediated c-di-GMP synthesis
-
physiological function
-
the enzyme synthesizes the central signaling molecule, cyclic diguanylate (c-di-GMP), which is found to regulate various bacterial phenotypes, especially those involved in pathogen infection and drug resistance. Enzyme PA0847 is an active diguanylate cyclase (DGC). Roles of PA0847 in the regulation of bacterial motility and biofilm formation. Enzyme PA0847 is involved in response to a variety of environmental nutrients and factors, suggesting it might serve as a broad-range environmental sensor on the membrane of Pseudomonas aeruginosa. Gene of PA0847 affects biofilm formation and motility phenotypes in Pseudomonas aeruginosa
-
physiological function
-
the primary signaling molecule promoting bacterial biofilm formation is the universal second messenger cyclic di-GMP. This dinucleotide predominantly controls the gene expression of motility, adhesins, and capsule production to coordinate biofilm formation. Cyclic di-GMP is synthesized by diguanylate cyclases (DGCs) that have a GGDEF domain and is degraded by phosphodiesterases (PDEs) containing either an EAL or an HD-GYP domain. The enzyme is important for the organism's biofilm formation ability, which plays a pivotal role in the virulence
-
physiological function
-
the primary signaling molecule promoting bacterial biofilm formation is the universal second messenger cyclic di-GMP. This dinucleotide predominantly controls the gene expression of motility, adhesins, and capsule production to coordinate biofilm formation. Cyclic di-GMP is synthesized by diguanylate cyclases (DGCs) that have a GGDEF domain and is degraded by phosphodiesterases (PDEs) containing either an EAL or an HD-GYP domain
-
physiological function
-
the primary signaling molecule promoting bacterial biofilm formation is the universal second messenger cyclic di-GMP. This dinucleotide predominantly controls the gene expression of motility, adhesins, and capsule production to coordinate biofilm formation. Cyclic di-GMP is synthesized by diguanylate cyclases (DGCs) that have a GGDEF domain and is degraded by phosphodiesterases (PDEs) containing either an EAL or an HD-GYP domain. The enzyme is important for the organism's biofilm formation ability, which plays a pivotal role in the virulence
-
physiological function
-
a deletion mutation in the pgn_1932 gene has a significant effect on the intracellular cyclic-di-GMP level in Porphyromonas gingivalis. Expression of the fimA and rgpA genes, encoding the major protein subunit of fimbriae and an arginine-specific proteinase, respectively, is downregulated in the pgn_1932 mutant. Correspondingly, FimA protein production and the fimbrial display on the mutant are significantly reduced. Mutations in the pgn_1932 gene also have a significant impact on the adhesive and invasive capabilities of P.orphyromonas gingivalis, which are required for its pathogenicity
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physiological function
-
Dcsbis tightly coordinates cell motility without markedly affecting biofilm formation and is a diguanylate cyclase with a catalytic activity much higher than those of many other diguanylate cyclases
-
physiological function
-
PA3177 is confirmed to be an active diguanylate cyclase, with overexpression affecting swimming and swarming motility, and inactivation affecting cellular bis-(3'-5')-cyclic dimeric GMP (c-di-GMP) levels of biofilm but not planktonic cells. PA3177 is confirmed to be an active diguanylate cyclase, with overexpression affecting swimming and swarming motility, and inactivation affecting cellular c-di-GMP levels of biofilm but not planktonic cells. While PA3177 contributes to biofilm drug tolerance, inactivation of PA3177 has no effect on attachment and biofilm formation
-
physiological function
-
cyclic diguanosine monophosphate (c-di-GMP) is one of the most important bacterial second messengers that controls many bacterial cellular functions including lifestyle switch between plankton and biofilm. Surface attachment defective (SadC) is a diguanylate cyclase (DGC) involved in the biosynthesis of c-di-GMP in Pseudomonas aeruginosa. SadC is reported to contribute to sensing of Psl and correspondingly increase of cellular c-di-GMP level. Involvement of Psl signalling in the SadC-mediated c-di-GMP synthesis
-
physiological function
-
the enzyme synthesizes the central signaling molecule, cyclic diguanylate (c-di-GMP), which is found to regulate various bacterial phenotypes, especially those involved in pathogen infection and drug resistance. Enzyme PA0847 is an active diguanylate cyclase (DGC). Roles of PA0847 in the regulation of bacterial motility and biofilm formation. Enzyme PA0847 is involved in response to a variety of environmental nutrients and factors, suggesting it might serve as a broad-range environmental sensor on the membrane of Pseudomonas aeruginosa. Gene of PA0847 affects biofilm formation and motility phenotypes in Pseudomonas aeruginosa
-
physiological function
-
the primary signaling molecule promoting bacterial biofilm formation is the universal second messenger cyclic di-GMP. This dinucleotide predominantly controls the gene expression of motility, adhesins, and capsule production to coordinate biofilm formation. Cyclic di-GMP is synthesized by diguanylate cyclases (DGCs) that have a GGDEF domain and is degraded by phosphodiesterases (PDEs) containing either an EAL or an HD-GYP domain. The enzyme is important for the organism's biofilm formation ability, which plays a pivotal role in the virulence
-
physiological function
-
the primary signaling molecule promoting bacterial biofilm formation is the universal second messenger cyclic di-GMP. This dinucleotide predominantly controls the gene expression of motility, adhesins, and capsule production to coordinate biofilm formation. Cyclic di-GMP is synthesized by diguanylate cyclases (DGCs) that have a GGDEF domain and is degraded by phosphodiesterases (PDEs) containing either an EAL or an HD-GYP domain
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physiological function
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ML1419c expression in Pseudomonas aeruginosa alters colony morphology, motility and biofilm formation in a manner consistent with increased cyclic di-GMP production. ML1419c expression increases cyclic di-GMP production in cultures in comparison to the vector control. The observed phenotypes and increased levels of cyclic di-GMP can be abrogated by mutation of the active site in ML1419c
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physiological function
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DgcA negatively affects virulence, extracellular polymeric substances production, bacterial autoaggregation and motility, but positively triggers biofilm formation via modulating the intracellular cyclic di-GMP levels. Deletion of dgcA substantially increases Xoo virulence against two different rice cultivars. 349 differentially expressed genes are controlled by DgcA
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physiological function
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DosD is a direct oxygen-sensing diguanylate cyclase playing a regulatory role in biofilm formation by Shewanella putrefaciens CN32 under aerobic conditions. The activity of DosD culminates to synthesis of cyclic diguanylate in the presence of oxygen. DosD regulates the transcription of the bpfA operon which encodes seven proteins including a large repetitive adhesin BpfA and its cognate type I secretion system (TISS). Regulation of DosD in aerobic biofilms is heavily dependent on an adhesin BpfA and the TISS
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physiological function
Vibrio cholerae serotype O1 C6706str2
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ectopic expression of VCA0965 in ibrio. cholerae causes a 3fold reduction in flagellar-based motility. An RXXD allosteric inhibition mutant of VCA0965 strongly inhibits motility and stimulates biofilm formation. This activity is lost when the active site of VCA0965 is mutated to AGDAF, suggesting that VCA0965 synthesizes cyclic-di-GMP. Ectopic expression of VCA0965 and VCA0965 containing a mutation in its RXXD motif significantly increases the intracellular cyclic-di-GMP levels in Vibrio cholerae and Escherichia coli. Purified VCA0965 is able to synthesize cyclic-di-GMP in vitro
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physiological function
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enzymic activity is dependent on the integrity of its GGDEF domain. Deletion of the dgcP gene shows that DgcP negatively regulates motility and positively controls biofilm formation, the deletion mutant mutant is hypovirulent in olive plants. Overexpression of the gene leads to an enhanced CR-binding phenotype that was accompanied by the formation of wrinkly colonies
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physiological function
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diguanylate cyclase (DGC) synthesizes the ubiquitous bacterial second messenger c-di-GMP. GcsA has no PDE activity. GcsA modulates the cellular c-di-GMP level at early exponential phase. Crosstalk between c-di-GMP and cAMP in the regulation of the expression of GcsA in Pseudomonas putida. GcsA plays a role in early biofilm formation of Pseudomonas putida and regulates the swimming motility in an FlgZ-dependent manner
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physiological function
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diguanylate cyclase (DGC) synthesizes the ubiquitous bacterial second messenger c-di-GMP. GcsA has no PDE activity. GcsA modulates the cellular c-di-GMP level at early exponential phase. Crosstalk between c-di-GMP and cAMP in the regulation of the expression of GcsA in Pseudomonas putida. GcsA plays a role in early biofilm formation of Pseudomonas putida and regulates the swimming motility in an FlgZ-dependent manner
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physiological function
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GcsA inhibits swimming motility in an FlgZ-dependent manner. The GGDEF domain of GcsA contains all the conserved signature amino acid residues that form the enzyme's active site, as well as other residues required for the diguanylate cyclase activity of the GGDEF domain. GcsA modulates the cellular cyclic di-GMP level at early exponential phase
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physiological function
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diguanylate cyclase (DGC) synthesizes the ubiquitous bacterial second messenger c-di-GMP. GcsA has no PDE activity. GcsA modulates the cellular c-di-GMP level at early exponential phase. Crosstalk between c-di-GMP and cAMP in the regulation of the expression of GcsA in Pseudomonas putida. GcsA plays a role in early biofilm formation of Pseudomonas putida and regulates the swimming motility in an FlgZ-dependent manner
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physiological function
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3',5'-cyclic diguanylate monophosphate (c-di-GMP) is a ubiquitous secondary messenger that plays a key role in response regulation and lifestyle conventions of pathogenic bacteria, including Vibrio cholerae. Increases in c-di-GMP levels induce increased expression of various factors necessary for the establishment and maintenance of biofilm communities, whereas decreased levels usually lead to enhanced expression of virulence and motility factors related to biofilm degradation. C-di-GMP is synthesized from guanosine triphosphate by diguanylate cyclase (DGC) enzymes
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physiological function
-
diguanylate cyclases in Vibrio cholerae are essential regulators of lifestyle switching, importance of DGCs and their product, cyclic-di-GMP, in the virulence and lifecycle of the bacteria. Biofilm formation in Vibrio cholerae empowers the bacteria to lead a dual lifestyle and enhances its infectivity. While the formation and dispersal of the biofilm involves multiple components, both proteinaceous and non-proteinaceous, the key to the regulatory control lies with the ubiquitous secondary signaling molecule, cyclic-di-GMP (c-di-GMP). Enzyme CdgD has a GGDEF domain along with a sensory PAS domain. It is a diguanylate cyclase. The enzyme does not have the conserved GGDEF motif, but has a degenerate AGDEF site. Significantly, expression of VCA0965 in Vibrio cholerae causes a 3fold reduction in flagellar-based motility. But enzyme VCA0965, despite its degenerate active site, synthesizes c-di-GMP
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physiological function
-
the primary signaling molecule promoting bacterial biofilm formation is the universal second messenger cyclic di-GMP. This dinucleotide predominantly controls the gene expression of motility, adhesins, and capsule production to coordinate biofilm formation. Cyclic di-GMP is synthesized by diguanylate cyclases (DGCs) that have a GGDEF domain and is degraded by phosphodiesterases (PDEs) containing either an EAL or an HD-GYP domain
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physiological function
-
3',5'-cyclic diguanylate monophosphate (c-di-GMP) is a ubiquitous secondary messenger that plays a key role in response regulation and lifestyle conventions of pathogenic bacteria, including Vibrio cholerae. Increases in c-di-GMP levels induce increased expression of various factors necessary for the establishment and maintenance of biofilm communities, whereas decreased levels usually lead to enhanced expression of virulence and motility factors related to biofilm degradation. C-di-GMP is synthesized from guanosine triphosphate by diguanylate cyclase (DGC) enzymes
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physiological function
-
diguanylate cyclases in Vibrio cholerae are essential regulators of lifestyle switching, importance of DGCs and their product, cyclic-di-GMP, in the virulence and lifecycle of the bacteria. Biofilm formation in Vibrio cholerae empowers the bacteria to lead a dual lifestyle and enhances its infectivity. While the formation and dispersal of the biofilm involves multiple components, both proteinaceous and non-proteinaceous, the key to the regulatory control lies with the ubiquitous secondary signaling molecule, cyclic-di-GMP (c-di-GMP). Enzyme CdgD has a GGDEF domain along with a sensory PAS domain. It is a diguanylate cyclase. The enzyme does not have the conserved GGDEF motif, but has a degenerate AGDEF site. Significantly, expression of VCA0965 in Vibrio cholerae causes a 3fold reduction in flagellar-based motility. But enzyme VCA0965, despite its degenerate active site, synthesizes c-di-GMP
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physiological function
-
the primary signaling molecule promoting bacterial biofilm formation is the universal second messenger cyclic di-GMP. This dinucleotide predominantly controls the gene expression of motility, adhesins, and capsule production to coordinate biofilm formation. Cyclic di-GMP is synthesized by diguanylate cyclases (DGCs) that have a GGDEF domain and is degraded by phosphodiesterases (PDEs) containing either an EAL or an HD-GYP domain
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physiological function
-
PA3177 is confirmed to be an active diguanylate cyclase, with overexpression affecting swimming and swarming motility, and inactivation affecting cellular bis-(3'-5')-cyclic dimeric GMP (c-di-GMP) levels of biofilm but not planktonic cells. PA3177 is confirmed to be an active diguanylate cyclase, with overexpression affecting swimming and swarming motility, and inactivation affecting cellular c-di-GMP levels of biofilm but not planktonic cells. While PA3177 contributes to biofilm drug tolerance, inactivation of PA3177 has no effect on attachment and biofilm formation
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physiological function
-
cyclic diguanosine monophosphate (c-di-GMP) is one of the most important bacterial second messengers that controls many bacterial cellular functions including lifestyle switch between plankton and biofilm. Surface attachment defective (SadC) is a diguanylate cyclase (DGC) involved in the biosynthesis of c-di-GMP in Pseudomonas aeruginosa. SadC is reported to contribute to sensing of Psl and correspondingly increase of cellular c-di-GMP level. Involvement of Psl signalling in the SadC-mediated c-di-GMP synthesis
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physiological function
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the enzyme synthesizes the central signaling molecule, cyclic diguanylate (c-di-GMP), which is found to regulate various bacterial phenotypes, especially those involved in pathogen infection and drug resistance. Enzyme PA0847 is an active diguanylate cyclase (DGC). Roles of PA0847 in the regulation of bacterial motility and biofilm formation. Enzyme PA0847 is involved in response to a variety of environmental nutrients and factors, suggesting it might serve as a broad-range environmental sensor on the membrane of Pseudomonas aeruginosa. Gene of PA0847 affects biofilm formation and motility phenotypes in Pseudomonas aeruginosa
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physiological function
-
the primary signaling molecule promoting bacterial biofilm formation is the universal second messenger cyclic di-GMP. This dinucleotide predominantly controls the gene expression of motility, adhesins, and capsule production to coordinate biofilm formation. Cyclic di-GMP is synthesized by diguanylate cyclases (DGCs) that have a GGDEF domain and is degraded by phosphodiesterases (PDEs) containing either an EAL or an HD-GYP domain. The enzyme is important for the organism's biofilm formation ability, which plays a pivotal role in the virulence
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physiological function
-
the primary signaling molecule promoting bacterial biofilm formation is the universal second messenger cyclic di-GMP. This dinucleotide predominantly controls the gene expression of motility, adhesins, and capsule production to coordinate biofilm formation. Cyclic di-GMP is synthesized by diguanylate cyclases (DGCs) that have a GGDEF domain and is degraded by phosphodiesterases (PDEs) containing either an EAL or an HD-GYP domain
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physiological function
-
PA3177 is confirmed to be an active diguanylate cyclase, with overexpression affecting swimming and swarming motility, and inactivation affecting cellular bis-(3'-5')-cyclic dimeric GMP (c-di-GMP) levels of biofilm but not planktonic cells. PA3177 is confirmed to be an active diguanylate cyclase, with overexpression affecting swimming and swarming motility, and inactivation affecting cellular c-di-GMP levels of biofilm but not planktonic cells. While PA3177 contributes to biofilm drug tolerance, inactivation of PA3177 has no effect on attachment and biofilm formation
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physiological function
-
cyclic diguanosine monophosphate (c-di-GMP) is one of the most important bacterial second messengers that controls many bacterial cellular functions including lifestyle switch between plankton and biofilm. Surface attachment defective (SadC) is a diguanylate cyclase (DGC) involved in the biosynthesis of c-di-GMP in Pseudomonas aeruginosa. SadC is reported to contribute to sensing of Psl and correspondingly increase of cellular c-di-GMP level. Involvement of Psl signalling in the SadC-mediated c-di-GMP synthesis
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physiological function
-
the enzyme synthesizes the central signaling molecule, cyclic diguanylate (c-di-GMP), which is found to regulate various bacterial phenotypes, especially those involved in pathogen infection and drug resistance. Enzyme PA0847 is an active diguanylate cyclase (DGC). Roles of PA0847 in the regulation of bacterial motility and biofilm formation. Enzyme PA0847 is involved in response to a variety of environmental nutrients and factors, suggesting it might serve as a broad-range environmental sensor on the membrane of Pseudomonas aeruginosa. Gene of PA0847 affects biofilm formation and motility phenotypes in Pseudomonas aeruginosa
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physiological function
-
the primary signaling molecule promoting bacterial biofilm formation is the universal second messenger cyclic di-GMP. This dinucleotide predominantly controls the gene expression of motility, adhesins, and capsule production to coordinate biofilm formation. Cyclic di-GMP is synthesized by diguanylate cyclases (DGCs) that have a GGDEF domain and is degraded by phosphodiesterases (PDEs) containing either an EAL or an HD-GYP domain. The enzyme is important for the organism's biofilm formation ability, which plays a pivotal role in the virulence
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physiological function
-
the primary signaling molecule promoting bacterial biofilm formation is the universal second messenger cyclic di-GMP. This dinucleotide predominantly controls the gene expression of motility, adhesins, and capsule production to coordinate biofilm formation. Cyclic di-GMP is synthesized by diguanylate cyclases (DGCs) that have a GGDEF domain and is degraded by phosphodiesterases (PDEs) containing either an EAL or an HD-GYP domain
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physiological function
-
PA3177 is confirmed to be an active diguanylate cyclase, with overexpression affecting swimming and swarming motility, and inactivation affecting cellular bis-(3'-5')-cyclic dimeric GMP (c-di-GMP) levels of biofilm but not planktonic cells. PA3177 is confirmed to be an active diguanylate cyclase, with overexpression affecting swimming and swarming motility, and inactivation affecting cellular c-di-GMP levels of biofilm but not planktonic cells. While PA3177 contributes to biofilm drug tolerance, inactivation of PA3177 has no effect on attachment and biofilm formation
-
physiological function
-
cyclic diguanosine monophosphate (c-di-GMP) is one of the most important bacterial second messengers that controls many bacterial cellular functions including lifestyle switch between plankton and biofilm. Surface attachment defective (SadC) is a diguanylate cyclase (DGC) involved in the biosynthesis of c-di-GMP in Pseudomonas aeruginosa. SadC is reported to contribute to sensing of Psl and correspondingly increase of cellular c-di-GMP level. Involvement of Psl signalling in the SadC-mediated c-di-GMP synthesis
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physiological function
-
the enzyme synthesizes the central signaling molecule, cyclic diguanylate (c-di-GMP), which is found to regulate various bacterial phenotypes, especially those involved in pathogen infection and drug resistance. Enzyme PA0847 is an active diguanylate cyclase (DGC). Roles of PA0847 in the regulation of bacterial motility and biofilm formation. Enzyme PA0847 is involved in response to a variety of environmental nutrients and factors, suggesting it might serve as a broad-range environmental sensor on the membrane of Pseudomonas aeruginosa. Gene of PA0847 affects biofilm formation and motility phenotypes in Pseudomonas aeruginosa
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physiological function
-
the primary signaling molecule promoting bacterial biofilm formation is the universal second messenger cyclic di-GMP. This dinucleotide predominantly controls the gene expression of motility, adhesins, and capsule production to coordinate biofilm formation. Cyclic di-GMP is synthesized by diguanylate cyclases (DGCs) that have a GGDEF domain and is degraded by phosphodiesterases (PDEs) containing either an EAL or an HD-GYP domain. The enzyme is important for the organism's biofilm formation ability, which plays a pivotal role in the virulence
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physiological function
-
the primary signaling molecule promoting bacterial biofilm formation is the universal second messenger cyclic di-GMP. This dinucleotide predominantly controls the gene expression of motility, adhesins, and capsule production to coordinate biofilm formation. Cyclic di-GMP is synthesized by diguanylate cyclases (DGCs) that have a GGDEF domain and is degraded by phosphodiesterases (PDEs) containing either an EAL or an HD-GYP domain
-
physiological function
-
PA3177 is confirmed to be an active diguanylate cyclase, with overexpression affecting swimming and swarming motility, and inactivation affecting cellular bis-(3'-5')-cyclic dimeric GMP (c-di-GMP) levels of biofilm but not planktonic cells. PA3177 is confirmed to be an active diguanylate cyclase, with overexpression affecting swimming and swarming motility, and inactivation affecting cellular c-di-GMP levels of biofilm but not planktonic cells. While PA3177 contributes to biofilm drug tolerance, inactivation of PA3177 has no effect on attachment and biofilm formation
-
physiological function
-
cyclic diguanosine monophosphate (c-di-GMP) is one of the most important bacterial second messengers that controls many bacterial cellular functions including lifestyle switch between plankton and biofilm. Surface attachment defective (SadC) is a diguanylate cyclase (DGC) involved in the biosynthesis of c-di-GMP in Pseudomonas aeruginosa. SadC is reported to contribute to sensing of Psl and correspondingly increase of cellular c-di-GMP level. Involvement of Psl signalling in the SadC-mediated c-di-GMP synthesis
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physiological function
-
the enzyme synthesizes the central signaling molecule, cyclic diguanylate (c-di-GMP), which is found to regulate various bacterial phenotypes, especially those involved in pathogen infection and drug resistance. Enzyme PA0847 is an active diguanylate cyclase (DGC). Roles of PA0847 in the regulation of bacterial motility and biofilm formation. Enzyme PA0847 is involved in response to a variety of environmental nutrients and factors, suggesting it might serve as a broad-range environmental sensor on the membrane of Pseudomonas aeruginosa. Gene of PA0847 affects biofilm formation and motility phenotypes in Pseudomonas aeruginosa
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physiological function
-
the primary signaling molecule promoting bacterial biofilm formation is the universal second messenger cyclic di-GMP. This dinucleotide predominantly controls the gene expression of motility, adhesins, and capsule production to coordinate biofilm formation. Cyclic di-GMP is synthesized by diguanylate cyclases (DGCs) that have a GGDEF domain and is degraded by phosphodiesterases (PDEs) containing either an EAL or an HD-GYP domain. The enzyme is important for the organism's biofilm formation ability, which plays a pivotal role in the virulence
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physiological function
-
the primary signaling molecule promoting bacterial biofilm formation is the universal second messenger cyclic di-GMP. This dinucleotide predominantly controls the gene expression of motility, adhesins, and capsule production to coordinate biofilm formation. Cyclic di-GMP is synthesized by diguanylate cyclases (DGCs) that have a GGDEF domain and is degraded by phosphodiesterases (PDEs) containing either an EAL or an HD-GYP domain
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physiological function
-
PA3177 is confirmed to be an active diguanylate cyclase, with overexpression affecting swimming and swarming motility, and inactivation affecting cellular bis-(3'-5')-cyclic dimeric GMP (c-di-GMP) levels of biofilm but not planktonic cells. PA3177 is confirmed to be an active diguanylate cyclase, with overexpression affecting swimming and swarming motility, and inactivation affecting cellular c-di-GMP levels of biofilm but not planktonic cells. While PA3177 contributes to biofilm drug tolerance, inactivation of PA3177 has no effect on attachment and biofilm formation
-
physiological function
-
cyclic diguanosine monophosphate (c-di-GMP) is one of the most important bacterial second messengers that controls many bacterial cellular functions including lifestyle switch between plankton and biofilm. Surface attachment defective (SadC) is a diguanylate cyclase (DGC) involved in the biosynthesis of c-di-GMP in Pseudomonas aeruginosa. SadC is reported to contribute to sensing of Psl and correspondingly increase of cellular c-di-GMP level. Involvement of Psl signalling in the SadC-mediated c-di-GMP synthesis
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physiological function
-
the enzyme synthesizes the central signaling molecule, cyclic diguanylate (c-di-GMP), which is found to regulate various bacterial phenotypes, especially those involved in pathogen infection and drug resistance. Enzyme PA0847 is an active diguanylate cyclase (DGC). Roles of PA0847 in the regulation of bacterial motility and biofilm formation. Enzyme PA0847 is involved in response to a variety of environmental nutrients and factors, suggesting it might serve as a broad-range environmental sensor on the membrane of Pseudomonas aeruginosa. Gene of PA0847 affects biofilm formation and motility phenotypes in Pseudomonas aeruginosa
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physiological function
-
the primary signaling molecule promoting bacterial biofilm formation is the universal second messenger cyclic di-GMP. This dinucleotide predominantly controls the gene expression of motility, adhesins, and capsule production to coordinate biofilm formation. Cyclic di-GMP is synthesized by diguanylate cyclases (DGCs) that have a GGDEF domain and is degraded by phosphodiesterases (PDEs) containing either an EAL or an HD-GYP domain. The enzyme is important for the organism's biofilm formation ability, which plays a pivotal role in the virulence
-
physiological function
-
the primary signaling molecule promoting bacterial biofilm formation is the universal second messenger cyclic di-GMP. This dinucleotide predominantly controls the gene expression of motility, adhesins, and capsule production to coordinate biofilm formation. Cyclic di-GMP is synthesized by diguanylate cyclases (DGCs) that have a GGDEF domain and is degraded by phosphodiesterases (PDEs) containing either an EAL or an HD-GYP domain
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physiological function
-
diguanylate cyclases in Vibrio cholerae are essential regulators of lifestyle switching, importance of DGCs and their product, cyclic-di-GMP, in the virulence and lifecycle of the bacteria. Biofilm formation in Vibrio cholerae empowers the bacteria to lead a dual lifestyle and enhances its infectivity. While the formation and dispersal of the biofilm involves multiple components, both proteinaceous and non-proteinaceous, the key to the regulatory control lies with the ubiquitous secondary signaling molecule, cyclic-di-GMP (c-di-GMP). Enzyme VC0395_0300 is a diguanylate cyclase with a GGEEF domain, it synthesizes c-di-GMP actively and has an essential role to play in the biofilm formation of Vibrio cholerae
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physiological function
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diguanylate cyclases in Vibrio cholerae are essential regulators of lifestyle switching, importance of DGCs and their product, cyclic-di-GMP, in the virulence and lifecycle of the bacteria. Biofilm formation in Vibrio cholerae empowers the bacteria to lead a dual lifestyle and enhances its infectivity. While the formation and dispersal of the biofilm involves multiple components, both proteinaceous and non-proteinaceous, the key to the regulatory control lies with the ubiquitous secondary signaling molecule, cyclic-di-GMP (c-di-GMP). Enzyme VC0395_0300 is a diguanylate cyclase with a GGEEF domain, it synthesizes c-di-GMP actively and has an essential role to play in the biofilm formation of Vibrio cholerae
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physiological function
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the primary signaling molecule promoting bacterial biofilm formation is the universal second messenger cyclic di-GMP. This dinucleotide predominantly controls the gene expression of motility, adhesins, and capsule production to coordinate biofilm formation. Cyclic di-GMP is synthesized by diguanylate cyclases (DGCs) that have a GGDEF domain and is degraded by phosphodiesterases (PDEs) containing either an EAL or an HD-GYP domain. The enzyme is important for the organism's biofilm formation ability, which plays a pivotal role in the virulence
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physiological function
-
the primary signaling molecule promoting bacterial biofilm formation is the universal second messenger cyclic di-GMP. This dinucleotide predominantly controls the gene expression of motility, adhesins, and capsule production to coordinate biofilm formation. Cyclic di-GMP is synthesized by diguanylate cyclases (DGCs) that have a GGDEF domain and is degraded by phosphodiesterases (PDEs) containing either an EAL or an HD-GYP domain
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physiological function
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the diguanylate cyclase AdrA regulates flagellar biosynthesis in Pseudomonas fluorescens F113 through SadB. AdrA is a diguanylate cyclase implicated in c-di-GMP-mediated cellulose production and biofilm formation. AdrA is involved in swimming and biofilm formation, since inactivation of the adrA gene results in increased swimming motility and a reduction in the initial stages of attachment to surfaces. The enzyme is implicated in flagellar gene expression, genetic interaction between adrA and sadB indicates that AdrA participates in the regulation of flagella biogenesis
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physiological function
Pseudomonas fluorescens Pfl01
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many bacteria contain large cyclic diguanylate (c-di-GMP) signaling networks made of diguanylate cyclases (DGCs) and phosphodiesterases that can direct cellular activities sensitive to c-di-GMP levels. While DGCs synthesize c-di-GMP, many DGCs also contain an autoinhibitory site (I-site) that binds c-di-GMP to halt excess production of this small molecule, thus controlling the amount of c-di-GMP available to bind to target proteins in the cell. Signaling between a DGC (GcbC) and its target protein (LapD) is a combined function of the I-site-dependent protein-protein interaction and the level of c-di-GMP production. The dual role of the I-site in modulating DGC activity as well as participating in protein-protein interactions suggests caution in interpreting the function of the I-site as only a means to negatively regulate a cyclase. These results implicate the I-site as an important positive and negative regulatory element of DGCs that may contribute to signaling specificity. Signaling specificity in Pseudomonas fluorescens is achieved by physical interaction is the regulation of biofilm formation by the inner membrane proteins GcbC and LapD. GcbC is a DGC that signals to the effector LapD. When bound to c-di-GMP, LapD changes conformation to sequester a periplasmic protease called LapG, thus allowing the large adhesin LapA to accumulate on the cell surface and thereby promoting biofilm formation
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physiological function
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diguanylate cyclases (DGCs) are responsible for the synthesis of second messenger cyclic di-guanosine monophosphate (c-di-GMP), which are involved in various physiological activities of bacterial species. DGC catalyzes the reaction of cyclic di-guanosine monophosphate (c-di-GMP) synthesis using guanosine triphosphate (GTP) as substrate. c-di-GMP is one of the potent regulator molecules, which is involved in many bacterial cellular functions, such as virulence, motility, bioluminescence, cellulose biosynthesis, adhesion, secretion, community behavior, biofilm formation, and cell differentiation
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additional information
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structure model of GST-DGC by the threading method, overview
additional information
the periplasmic portion of CdgH forms a homodimer in solution which undergoes conformational changes upon L-arginine binding. Homodimerization leads to alignment of the two GGDEF domains, resulting in 2fold symmetry that enables the enzyme to catalyze c-diGMP synthesis. Both tandem PBPb domains of CdgH contain a typical interlobe ligand-binding structural architecture. PBPb-I and -II domains have different amino acid binding specificity. The PBPb-I domain is primarily an L-arginine/L-lysine/L-ornithine-binding domain, whereas the PBPb-II domain exhibits a preference for L-glutamine and L-histidine, binding site structures, overview. Comparison of the CdgH PBPb-I domain with other amino acid-binding proteins
additional information
DGCs operate as dimers, using their GGDEF domains to produce c-di-GMP. In addition to GGDEF, active cyclases have also been found that make use of GGEEF, AGDEF, and GGDEM motifs
additional information
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DGCs operate as dimers, using their GGDEF domains to produce c-di-GMP. In addition to GGDEF, active cyclases have also been found that make use of GGEEF, AGDEF, and GGDEM motifs
additional information
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DGCs operate as dimers, using their GGDEF domains to produce c-di-GMP. In addition to GGDEF, active cyclases have also been found that make use of GGEEF, AGDEF, and GGDEM motifs
additional information
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DGCs operate as dimers, using their GGDEF domains to produce c-di-GMP. In addition to GGDEF, active cyclases have also been found that make use of GGEEF, AGDEF, and GGDEM motifs
additional information
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DGCs operate as dimers, using their GGDEF domains to produce c-di-GMP. In addition to GGDEF, active cyclases have also been found that make use of GGEEF, AGDEF, and GGDEM motifs
additional information
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DGCs operate as dimers, using their GGDEF domains to produce c-di-GMP. In addition to GGDEF, active cyclases have also been found that make use of GGEEF, AGDEF, and GGDEM motifs
additional information
DGCs operate as dimers, using their GGDEF domains to produce c-di-GMP. In addition to GGDEF, active cyclases have also been found that make use of GGEEF, AGDEF, and GGDEM motifs
additional information
the GGDEF domain of SadC has a typical GGDEF structure and the alpha-helix connecting the transmembrane domains with SadC GGDEF domain is essential for SadC to form DGC oligomers. Membrane association of SadC promotes its DGC activity by affecting the formation of active DGC oligomers. The GGDEF domain of SadC has a typical GGDEF structure
additional information
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the GGDEF domain of SadC has a typical GGDEF structure and the alpha-helix connecting the transmembrane domains with SadC GGDEF domain is essential for SadC to form DGC oligomers. Membrane association of SadC promotes its DGC activity by affecting the formation of active DGC oligomers. The GGDEF domain of SadC has a typical GGDEF structure
additional information
the diguanylate cyclase activity of PA0847 depends on the neighboring PAS domain. A local structural change imposed by an adjacent tyrosine residue is identified, which indicates the structural and functional diversities of the GGDEF family proteins. Signaling mechanism of the unique c-di-GMP metabolizing protein PA0847, overview. Three-dimensional homology model of PA0847 GGDEF domain (residues 576-736) using DGC DgcZ (PDB ID 4H54) as a structure template. Seven critical residues, D609, K614, N617, D626, D652, E653, and K722, are involved in GTP binding
additional information
the autoinhibitory I-site of a diguanylate cyclase is a necessary element for interaction and signaling with an effector protein
additional information
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the autoinhibitory I-site of a diguanylate cyclase is a necessary element for interaction and signaling with an effector protein
additional information
enzyme Lcd1 has an N-terminal cGMP-specific phosphodiesterase domain, an adenylyl cyclase domain, a FhlA (GAF) domain, and a C-terminal GGDEF domain. The GAF domain regulates the DGC activity of Lcd1. The GAF domain binds specifically cAMP and has animportant role in the regulation of the DGC activity of the GGDEF domain. Lcd1 DGC activity is negligible in the absence of cAMP and is significantly enhanced in its presence. Structure comparison, overview
additional information
in blue light, wild-type cells are sessile while DELTAcph2 cells move towards the light source. The product of the gene cph2 is a photosensory protein, Cph2, which consists of six domains with the architecture GAF-GAF-GGDEF-EAL-CBCR-GGDEF (GAF, cGMP phosphodiesterase/adenylyl cylase/FhlA, CBCR, cyanobacteriochrome, GGDEF, degenerate motif). The domains 1 (GAF) and 5 (CBCR) covalently bind phycocyanobilin (PCB) as a chromophore, allowing the absorbance of light in the visible spectrum
additional information
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the structure of CdgH is solved and displays the presence of two N-terminal tandem periplasmic substrate-binding (PBPb) domains for signal recognition
additional information
binding mode of the substrate analogue GTP-alpha-S (guanosine-alpha-thio-triphosphate) bound to PleD
additional information
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binding mode of the substrate analogue GTP-alpha-S (guanosine-alpha-thio-triphosphate) bound to PleD
additional information
binding mode of the substrate analogue GTP-alpha-S (guanosine-alpha-thio-triphosphate) bound to PleD
additional information
binding mode of the substrate analogue GTP-alpha-S (guanosine-alpha-thio-triphosphate) bound to PleD
additional information
the enzyme's diguanylate cyclase activity requires an intact globin domain. In the distal heme pocket of the globin domain, residues Phe42, Tyr43, Ala68, and Met69 are required to maintain full diguanylate cyclase activity. The highly conserved amino acids His223 and Lys224 in the middle domain of EcGReg are essential to diguanylate cyclase activity. Sixteen important residues (Leu300, Arg306, Asp333, Phe337, Lys338, Asn341, Asp342, Asp350, Leu353, Asp368, Arg372, Gly374, Gly375, Asp376, Glu377, and Phe378) are identified in the active site and inhibitory site of the diguanylate cyclase domain of EcGReg
additional information
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the enzyme's diguanylate cyclase activity requires an intact globin domain. In the distal heme pocket of the globin domain, residues Phe42, Tyr43, Ala68, and Met69 are required to maintain full diguanylate cyclase activity. The highly conserved amino acids His223 and Lys224 in the middle domain of EcGReg are essential to diguanylate cyclase activity. Sixteen important residues (Leu300, Arg306, Asp333, Phe337, Lys338, Asn341, Asp342, Asp350, Leu353, Asp368, Arg372, Gly374, Gly375, Asp376, Glu377, and Phe378) are identified in the active site and inhibitory site of the diguanylate cyclase domain of EcGReg
additional information
the enzyme's diguanylate cyclase activity requires an intact globin domain. In the distal heme pocket of the globin domain, residues Phe42, Tyr43, Ser68, and Met69 are required to maintain full diguanylatecyclase activity. The highly conserved amino acids His225 and Lys226 in the middle domain of BpeGReg are essential to diguanylate cyclase activity. Bpe-GReg may interact with other c-di-GMP-metabolizing proteins to form mixed signaling teams
additional information
-
the enzyme's diguanylate cyclase activity requires an intact globin domain. In the distal heme pocket of the globin domain, residues Phe42, Tyr43, Ser68, and Met69 are required to maintain full diguanylatecyclase activity. The highly conserved amino acids His225 and Lys226 in the middle domain of BpeGReg are essential to diguanylate cyclase activity. Bpe-GReg may interact with other c-di-GMP-metabolizing proteins to form mixed signaling teams
additional information
-
the enzyme's diguanylate cyclase activity requires an intact globin domain. In the distal heme pocket of the globin domain, residues Phe42, Tyr43, Ser68, and Met69 are required to maintain full diguanylatecyclase activity. The highly conserved amino acids His225 and Lys226 in the middle domain of BpeGReg are essential to diguanylate cyclase activity. Bpe-GReg may interact with other c-di-GMP-metabolizing proteins to form mixed signaling teams
-
additional information
-
binding mode of the substrate analogue GTP-alpha-S (guanosine-alpha-thio-triphosphate) bound to PleD
-
additional information
-
the GGDEF domain of SadC has a typical GGDEF structure and the alpha-helix connecting the transmembrane domains with SadC GGDEF domain is essential for SadC to form DGC oligomers. Membrane association of SadC promotes its DGC activity by affecting the formation of active DGC oligomers. The GGDEF domain of SadC has a typical GGDEF structure
-
additional information
-
the diguanylate cyclase activity of PA0847 depends on the neighboring PAS domain. A local structural change imposed by an adjacent tyrosine residue is identified, which indicates the structural and functional diversities of the GGDEF family proteins. Signaling mechanism of the unique c-di-GMP metabolizing protein PA0847, overview. Three-dimensional homology model of PA0847 GGDEF domain (residues 576-736) using DGC DgcZ (PDB ID 4H54) as a structure template. Seven critical residues, D609, K614, N617, D626, D652, E653, and K722, are involved in GTP binding
-
additional information
-
binding mode of the substrate analogue GTP-alpha-S (guanosine-alpha-thio-triphosphate) bound to PleD
-
additional information
-
the GGDEF domain of SadC has a typical GGDEF structure and the alpha-helix connecting the transmembrane domains with SadC GGDEF domain is essential for SadC to form DGC oligomers. Membrane association of SadC promotes its DGC activity by affecting the formation of active DGC oligomers. The GGDEF domain of SadC has a typical GGDEF structure
-
additional information
-
the diguanylate cyclase activity of PA0847 depends on the neighboring PAS domain. A local structural change imposed by an adjacent tyrosine residue is identified, which indicates the structural and functional diversities of the GGDEF family proteins. Signaling mechanism of the unique c-di-GMP metabolizing protein PA0847, overview. Three-dimensional homology model of PA0847 GGDEF domain (residues 576-736) using DGC DgcZ (PDB ID 4H54) as a structure template. Seven critical residues, D609, K614, N617, D626, D652, E653, and K722, are involved in GTP binding
-
additional information
-
binding mode of the substrate analogue GTP-alpha-S (guanosine-alpha-thio-triphosphate) bound to PleD
-
additional information
-
binding mode of the substrate analogue GTP-alpha-S (guanosine-alpha-thio-triphosphate) bound to PleD
-
additional information
-
the periplasmic portion of CdgH forms a homodimer in solution which undergoes conformational changes upon L-arginine binding. Homodimerization leads to alignment of the two GGDEF domains, resulting in 2fold symmetry that enables the enzyme to catalyze c-diGMP synthesis. Both tandem PBPb domains of CdgH contain a typical interlobe ligand-binding structural architecture. PBPb-I and -II domains have different amino acid binding specificity. The PBPb-I domain is primarily an L-arginine/L-lysine/L-ornithine-binding domain, whereas the PBPb-II domain exhibits a preference for L-glutamine and L-histidine, binding site structures, overview. Comparison of the CdgH PBPb-I domain with other amino acid-binding proteins
-
additional information
-
the periplasmic portion of CdgH forms a homodimer in solution which undergoes conformational changes upon L-arginine binding. Homodimerization leads to alignment of the two GGDEF domains, resulting in 2fold symmetry that enables the enzyme to catalyze c-diGMP synthesis. Both tandem PBPb domains of CdgH contain a typical interlobe ligand-binding structural architecture. PBPb-I and -II domains have different amino acid binding specificity. The PBPb-I domain is primarily an L-arginine/L-lysine/L-ornithine-binding domain, whereas the PBPb-II domain exhibits a preference for L-glutamine and L-histidine, binding site structures, overview. Comparison of the CdgH PBPb-I domain with other amino acid-binding proteins
-
additional information
-
the GGDEF domain of SadC has a typical GGDEF structure and the alpha-helix connecting the transmembrane domains with SadC GGDEF domain is essential for SadC to form DGC oligomers. Membrane association of SadC promotes its DGC activity by affecting the formation of active DGC oligomers. The GGDEF domain of SadC has a typical GGDEF structure
-
additional information
-
the diguanylate cyclase activity of PA0847 depends on the neighboring PAS domain. A local structural change imposed by an adjacent tyrosine residue is identified, which indicates the structural and functional diversities of the GGDEF family proteins. Signaling mechanism of the unique c-di-GMP metabolizing protein PA0847, overview. Three-dimensional homology model of PA0847 GGDEF domain (residues 576-736) using DGC DgcZ (PDB ID 4H54) as a structure template. Seven critical residues, D609, K614, N617, D626, D652, E653, and K722, are involved in GTP binding
-
additional information
-
binding mode of the substrate analogue GTP-alpha-S (guanosine-alpha-thio-triphosphate) bound to PleD
-
additional information
-
the GGDEF domain of SadC has a typical GGDEF structure and the alpha-helix connecting the transmembrane domains with SadC GGDEF domain is essential for SadC to form DGC oligomers. Membrane association of SadC promotes its DGC activity by affecting the formation of active DGC oligomers. The GGDEF domain of SadC has a typical GGDEF structure
-
additional information
-
the diguanylate cyclase activity of PA0847 depends on the neighboring PAS domain. A local structural change imposed by an adjacent tyrosine residue is identified, which indicates the structural and functional diversities of the GGDEF family proteins. Signaling mechanism of the unique c-di-GMP metabolizing protein PA0847, overview. Three-dimensional homology model of PA0847 GGDEF domain (residues 576-736) using DGC DgcZ (PDB ID 4H54) as a structure template. Seven critical residues, D609, K614, N617, D626, D652, E653, and K722, are involved in GTP binding
-
additional information
-
binding mode of the substrate analogue GTP-alpha-S (guanosine-alpha-thio-triphosphate) bound to PleD
-
additional information
-
the GGDEF domain of SadC has a typical GGDEF structure and the alpha-helix connecting the transmembrane domains with SadC GGDEF domain is essential for SadC to form DGC oligomers. Membrane association of SadC promotes its DGC activity by affecting the formation of active DGC oligomers. The GGDEF domain of SadC has a typical GGDEF structure
-
additional information
-
the diguanylate cyclase activity of PA0847 depends on the neighboring PAS domain. A local structural change imposed by an adjacent tyrosine residue is identified, which indicates the structural and functional diversities of the GGDEF family proteins. Signaling mechanism of the unique c-di-GMP metabolizing protein PA0847, overview. Three-dimensional homology model of PA0847 GGDEF domain (residues 576-736) using DGC DgcZ (PDB ID 4H54) as a structure template. Seven critical residues, D609, K614, N617, D626, D652, E653, and K722, are involved in GTP binding
-
additional information
-
binding mode of the substrate analogue GTP-alpha-S (guanosine-alpha-thio-triphosphate) bound to PleD
-
additional information
-
the GGDEF domain of SadC has a typical GGDEF structure and the alpha-helix connecting the transmembrane domains with SadC GGDEF domain is essential for SadC to form DGC oligomers. Membrane association of SadC promotes its DGC activity by affecting the formation of active DGC oligomers. The GGDEF domain of SadC has a typical GGDEF structure
-
additional information
-
the diguanylate cyclase activity of PA0847 depends on the neighboring PAS domain. A local structural change imposed by an adjacent tyrosine residue is identified, which indicates the structural and functional diversities of the GGDEF family proteins. Signaling mechanism of the unique c-di-GMP metabolizing protein PA0847, overview. Three-dimensional homology model of PA0847 GGDEF domain (residues 576-736) using DGC DgcZ (PDB ID 4H54) as a structure template. Seven critical residues, D609, K614, N617, D626, D652, E653, and K722, are involved in GTP binding
-
additional information
-
binding mode of the substrate analogue GTP-alpha-S (guanosine-alpha-thio-triphosphate) bound to PleD
-
additional information
-
the GGDEF domain of SadC has a typical GGDEF structure and the alpha-helix connecting the transmembrane domains with SadC GGDEF domain is essential for SadC to form DGC oligomers. Membrane association of SadC promotes its DGC activity by affecting the formation of active DGC oligomers. The GGDEF domain of SadC has a typical GGDEF structure
-
additional information
-
the diguanylate cyclase activity of PA0847 depends on the neighboring PAS domain. A local structural change imposed by an adjacent tyrosine residue is identified, which indicates the structural and functional diversities of the GGDEF family proteins. Signaling mechanism of the unique c-di-GMP metabolizing protein PA0847, overview. Three-dimensional homology model of PA0847 GGDEF domain (residues 576-736) using DGC DgcZ (PDB ID 4H54) as a structure template. Seven critical residues, D609, K614, N617, D626, D652, E653, and K722, are involved in GTP binding
-
additional information
-
binding mode of the substrate analogue GTP-alpha-S (guanosine-alpha-thio-triphosphate) bound to PleD
-
additional information
-
the enzyme's diguanylate cyclase activity requires an intact globin domain. In the distal heme pocket of the globin domain, residues Phe42, Tyr43, Ser68, and Met69 are required to maintain full diguanylatecyclase activity. The highly conserved amino acids His225 and Lys226 in the middle domain of BpeGReg are essential to diguanylate cyclase activity. Bpe-GReg may interact with other c-di-GMP-metabolizing proteins to form mixed signaling teams
-
additional information
Pseudomonas fluorescens Pfl01
-
the autoinhibitory I-site of a diguanylate cyclase is a necessary element for interaction and signaling with an effector protein
-
additional information
-
the enzyme's diguanylate cyclase activity requires an intact globin domain. In the distal heme pocket of the globin domain, residues Phe42, Tyr43, Ser68, and Met69 are required to maintain full diguanylatecyclase activity. The highly conserved amino acids His225 and Lys226 in the middle domain of BpeGReg are essential to diguanylate cyclase activity. Bpe-GReg may interact with other c-di-GMP-metabolizing proteins to form mixed signaling teams
-
additional information
-
structure model of GST-DGC by the threading method, overview
-
additional information
Vibrio cholerae serotype O1 A1552
-
DGCs operate as dimers, using their GGDEF domains to produce c-di-GMP. In addition to GGDEF, active cyclases have also been found that make use of GGEEF, AGDEF, and GGDEM motifs
-
Show AA Sequence and Transmembrane Helices (83748 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
101600
dimeric periplasmic portion of enzyme CdgH, sequence calculation
161200
-
mutant R198/242A, coupled gel-filtration/multiangle light scattering, tetramer
161300
-
mutant L170D, coupled gel-filtration/multiangle light scattering, tetramer
161600
-
mutant R198A, coupled gel-filtration/multiangle light scattering, tetramer
162100
-
mutant R242A, coupled gel-filtration/multiangle light scattering, tetramer
162700
-
GGAAF mutant, coupled gel-filtration/multiangle light scattering, tetramer
22300
monomeric PBPbI domain, analytical ultracentrifugation
39170
50000
DosC purified from Escherichia coli moderately overexpressing the wild-type dosCP operon, determined by SDS-PAGE
52000
55000
-
mutant L167D, gel-filtration, monomer or weakly associated dimer
56000
recombinant PleD, determined by SDS-PAGE and Western Blot analysis
73300
-
mutant L170D, coupled gel-filtration/multiangle light scattering, tetramer
76000
78600
-
mutant R242A, coupled gel-filtration/multiangle light scattering, dimer
80100
-
mutant R198/242A, coupled gel-filtration/multiangle light scattering, dimer
81300
85900
-
wild-type, coupled gel-filtration/multiangle light scattering, dimer
87300
recombinant dimeric periplasmic portion of enzyme CdgH, analytical ultracentrifugation
52000
native Anaplasma phagocytophilum PleD, determined by SDS-PAGE and Western Blot analysis
81300
-
wild-type (phosphodiesterase-treated) and GGAAF mutant, coupled gel-filtration/multiangle light scattering, dimer
81300
-
mutant R198A, coupled gel-filtration/multiangle light scattering, dimer
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homotetramer
octamer
tetramer
additional information
dimer
at high protein concentrations and/or presence of divalent metal ions (Mg2+, Mn2+), tightened upon BeF3-modification, exothermic dimerisation, KD: 100 microM, gel filtration chromatography and crystallography
dimer
enzymatically active state, concentration dependent, crosslinking (using disuccinimidyl suberate, DSS)
dimer
2 * 37600, apoform Lcd1GAF domain, SDS-PAGE, 2 * 37700, Lcd1GAF domain in complex with cAMP, SDS-PAGE
dimer
-
compact structure, globular shape, active state, phosphodiesterase-treated (hydrolysis of bound cyclic di-3,5-guanylate) and nucleotide-free wild-type, nucleotide-free mutants GGAAF, R242A and R198A and cyclic di-3,5-guanylate-bound mutant L170D, coupled gel-filtration/multiangle light scattering
dimer
-
elongated shape, product-inhibited state, purified wild-type (cyclic di-3,5-guanylate-bound), coupled gel-filtration/multiangle light scattering
dimer
domain analysis of PA0847 shows a unique molecular architecture with an N-terminal periplasmic sensory domain and a C-terminal intracellular GGDEF domain. Structural model of PA0847 GGDEF dimer, overview
dimer
-
domain analysis of PA0847 shows a unique molecular architecture with an N-terminal periplasmic sensory domain and a C-terminal intracellular GGDEF domain. Structural model of PA0847 GGDEF dimer, overview
-
dimer
-
domain analysis of PA0847 shows a unique molecular architecture with an N-terminal periplasmic sensory domain and a C-terminal intracellular GGDEF domain. Structural model of PA0847 GGDEF dimer, overview
-
dimer
-
domain analysis of PA0847 shows a unique molecular architecture with an N-terminal periplasmic sensory domain and a C-terminal intracellular GGDEF domain. Structural model of PA0847 GGDEF dimer, overview
-
dimer
-
domain analysis of PA0847 shows a unique molecular architecture with an N-terminal periplasmic sensory domain and a C-terminal intracellular GGDEF domain. Structural model of PA0847 GGDEF dimer, overview
-
dimer
-
domain analysis of PA0847 shows a unique molecular architecture with an N-terminal periplasmic sensory domain and a C-terminal intracellular GGDEF domain. Structural model of PA0847 GGDEF dimer, overview
-
dimer
-
domain analysis of PA0847 shows a unique molecular architecture with an N-terminal periplasmic sensory domain and a C-terminal intracellular GGDEF domain. Structural model of PA0847 GGDEF dimer, overview
-
dimer
-
domain analysis of PA0847 shows a unique molecular architecture with an N-terminal periplasmic sensory domain and a C-terminal intracellular GGDEF domain. Structural model of PA0847 GGDEF dimer, overview
-
dimer
-
compact structure, globular shape, active state, phosphodiesterase-treated (hydrolysis of bound cyclic di-3,5-guanylate) and nucleotide-free wild-type, coupled gel-filtration/multiangle light scattering
dimer
-
elongated shape, product-inhibited state, purified wild-type (cyclic di-3,5-guanylate-bound), coupled gel-filtration/multiangle light scattering
dimer
-
compact structure, globular shape, active state, phosphodiesterase-treated (hydrolysis of bound cyclic di-3,5-guanylate) and nucleotide-free wild-type, coupled gel-filtration/multiangle light scattering
-
dimer
-
elongated shape, product-inhibited state, purified wild-type (cyclic di-3,5-guanylate-bound), coupled gel-filtration/multiangle light scattering
-
dimer
-
compact structure, globular shape, active state, phosphodiesterase-treated (hydrolysis of bound cyclic di-3,5-guanylate) and nucleotide-free wild-type, coupled gel-filtration/multiangle light scattering
dimer
-
elongated shape, product-inhibited state, purified wild-type (cyclic di-3,5-guanylate-bound), coupled gel-filtration/multiangle light scattering
dimer
-
compact structure, globular shape, active state, phosphodiesterase-treated (hydrolysis of bound cyclic di-3,5-guanylate) and nucleotide-free wild-type, coupled gel-filtration/multiangle light scattering
-
dimer
-
elongated shape, product-inhibited state, purified wild-type (cyclic di-3,5-guanylate-bound), coupled gel-filtration/multiangle light scattering
-
dimer
-
compact structure, globular shape, active state, phosphodiesterase-treated (hydrolysis of bound cyclic di-3,5-guanylate) and nucleotide-free wild-type, coupled gel-filtration/multiangle light scattering
dimer
-
elongated shape, product-inhibited state, purified wild-type (cyclic di-3,5-guanylate-bound), coupled gel-filtration/multiangle light scattering
dimer
-
compact structure, globular shape, active state, phosphodiesterase-treated (hydrolysis of bound cyclic di-3,5-guanylate) and nucleotide-free wild-type, coupled gel-filtration/multiangle light scattering
-
dimer
-
elongated shape, product-inhibited state, purified wild-type (cyclic di-3,5-guanylate-bound), coupled gel-filtration/multiangle light scattering
-
octamer
-
8 * 71900, recombinant GST-tagged enzyme, SDS- and native PAGE, and LC-MS/MS, 8 * 73000, about, sequence calculation
octamer
-
8 * 71900, recombinant GST-tagged enzyme, SDS- and native PAGE, and LC-MS/MS, 8 * 73000, about, sequence calculation
-
tetramer
-
transient intermediate state between active, compact dimer and product-inhibited, elongated dimer, induced by high enzyme concentration, nucleotide-depleted wild-type sample, nucleotide-free mutants GGAAF, R242A and R198A and cyclic di-3,5-guanylate-bound mutant L170D, crystallography, coupled gel-filtration/multiangle light scattering
tetramer
-
transient intermediate state between active, compact dimer and product-inhibited, elongated dimer, induced by high enzyme concentration, nucleotide-depleted wild-type, coupled gel-filtration/multiangle light scattering
tetramer
-
transient intermediate state between active, compact dimer and product-inhibited, elongated dimer, induced by high enzyme concentration, nucleotide-depleted wild-type, coupled gel-filtration/multiangle light scattering
-
tetramer
-
transient intermediate state between active, compact dimer and product-inhibited, elongated dimer, induced by high enzyme concentration, nucleotide-depleted wild-type, coupled gel-filtration/multiangle light scattering
tetramer
-
transient intermediate state between active, compact dimer and product-inhibited, elongated dimer, induced by high enzyme concentration, nucleotide-depleted wild-type, coupled gel-filtration/multiangle light scattering
-
tetramer
-
transient intermediate state between active, compact dimer and product-inhibited, elongated dimer, induced by high enzyme concentration, nucleotide-depleted wild-type, coupled gel-filtration/multiangle light scattering
tetramer
-
transient intermediate state between active, compact dimer and product-inhibited, elongated dimer, induced by high enzyme concentration, nucleotide-depleted wild-type, coupled gel-filtration/multiangle light scattering
-
additional information
-
the GGDEF domain is sufficient to encode catalytic activity, which is highly regulated by the adjacent sensory protein domain
additional information
-
dimer is the catalytically active state of enzyme
additional information
dimer is the catalytically active state of enzyme
additional information
-
the GGDEF domain is sufficient to encode catalytic activity, which is highly regulated by the adjacent sensory protein domain
additional information
Cereibacter sphaeroides RSP3513
-
the GGDEF domain is sufficient to encode catalytic activity, which is highly regulated by the adjacent sensory protein domain
-
additional information
-
the GGDEF domain is responsible for the diguanylate cyclase activity
additional information
the inactive heme-free H93A mutant is primarily octameric, suggesting that catalytically active dimer formation requires heme binding. The dimer to tetramer ratios for MBP-tagged YddV in the presence and absence of GTP (and therefore of c-di-GMP) are 3.7:1 and 4.3:1, respectively. Like the Fe(III) form, the Fe(II)-O2, Fe(III)-CN- and Fe(III)-imidazole forms of YddV-MBP exist primarily as dimers, with tetramers being minor components
additional information
-
the inactive heme-free H93A mutant is primarily octameric, suggesting that catalytically active dimer formation requires heme binding. The dimer to tetramer ratios for MBP-tagged YddV in the presence and absence of GTP (and therefore of c-di-GMP) are 3.7:1 and 4.3:1, respectively. Like the Fe(III) form, the Fe(II)-O2, Fe(III)-CN- and Fe(III)-imidazole forms of YddV-MBP exist primarily as dimers, with tetramers being minor components
additional information
-
the GGDEF domain is responsible for the diguanylate cyclase activity
additional information
enzyme Lcd1 has an N-terminal cGMP-specific phosphodiesterase domain, an adenylyl cyclase domain, a FhlA (GAF) domain, and a C-terminal GGDEF domain. The N-terminal GAF domain comprises residues 28-165 and the C-terminal GGDEF domain residues 178-326, with a predicted linker (residues 166-177) between them. The full-length Lcd1 and its GAF domain form dimers in solution. The dimer interface involves 48 residues, mainly from alpha1 and alpha6. The dimerization interface involves many hydrogen bonds. On their own, these intermolecular H-bonds can be replaced with protein-solvent hydrogen bonds with little energetic penalty if it is not for additional intersubunit interactions involving hydrophobic and aromatic residues I11, Y14, L25, V152, F160, I162, H167, and Y171. In the full-length protein, the C-terminus of the GAF domain is linked to the N-terminus of the GGDEF domain. In the Lcd1GAF-cAMP dimer, the two C-terminal alpha6 helices are pointing in the same direction, and the Calpha atoms of the C-terminal T174 residues are separated by only 6.4 A
additional information
protein PGN_1932 contains a GGDEF domain
additional information
-
protein PGN_1932 contains a GGDEF domain
-
additional information
-
higher-order oligomerisation depends on interactions of stalk motifs
additional information
-
compact and elongated dimeric conformation correspond to catalytically active and inactive state, respectively
additional information
full-length Dcsbis protein contains an N-terminal GAF domain and a C-terminal GGDEF domain
additional information
-
full-length Dcsbis protein contains an N-terminal GAF domain and a C-terminal GGDEF domain
additional information
the GGDEF domain of SadC has a typical GGDEF structure and the alpha-helix connecting the transmembrane domains with SadC GGDEF domain is essential for SadC to form DGC oligomers. Membrane association of SadC promotes its DGC activity by affecting the formation of active DGC oligomers. The alpha-helix of amino acid residues 300-322 is necessary for SadC300-487 to form active hexamers, hexameric and monomeric structures. The structure of SadC323-487 contains five beta-sheets sandwiched by five alpha-helices, which is a typical GGDEF structure. Enzyme mutants structure-function analysis, overview
additional information
-
the GGDEF domain of SadC has a typical GGDEF structure and the alpha-helix connecting the transmembrane domains with SadC GGDEF domain is essential for SadC to form DGC oligomers. Membrane association of SadC promotes its DGC activity by affecting the formation of active DGC oligomers. The alpha-helix of amino acid residues 300-322 is necessary for SadC300-487 to form active hexamers, hexameric and monomeric structures. The structure of SadC323-487 contains five beta-sheets sandwiched by five alpha-helices, which is a typical GGDEF structure. Enzyme mutants structure-function analysis, overview
additional information
-
the GGDEF domain of SadC has a typical GGDEF structure and the alpha-helix connecting the transmembrane domains with SadC GGDEF domain is essential for SadC to form DGC oligomers. Membrane association of SadC promotes its DGC activity by affecting the formation of active DGC oligomers. The alpha-helix of amino acid residues 300-322 is necessary for SadC300-487 to form active hexamers, hexameric and monomeric structures. The structure of SadC323-487 contains five beta-sheets sandwiched by five alpha-helices, which is a typical GGDEF structure. Enzyme mutants structure-function analysis, overview
-
additional information
-
the GGDEF domain of SadC has a typical GGDEF structure and the alpha-helix connecting the transmembrane domains with SadC GGDEF domain is essential for SadC to form DGC oligomers. Membrane association of SadC promotes its DGC activity by affecting the formation of active DGC oligomers. The alpha-helix of amino acid residues 300-322 is necessary for SadC300-487 to form active hexamers, hexameric and monomeric structures. The structure of SadC323-487 contains five beta-sheets sandwiched by five alpha-helices, which is a typical GGDEF structure. Enzyme mutants structure-function analysis, overview
-
additional information
-
the GGDEF domain of SadC has a typical GGDEF structure and the alpha-helix connecting the transmembrane domains with SadC GGDEF domain is essential for SadC to form DGC oligomers. Membrane association of SadC promotes its DGC activity by affecting the formation of active DGC oligomers. The alpha-helix of amino acid residues 300-322 is necessary for SadC300-487 to form active hexamers, hexameric and monomeric structures. The structure of SadC323-487 contains five beta-sheets sandwiched by five alpha-helices, which is a typical GGDEF structure. Enzyme mutants structure-function analysis, overview
-
additional information
-
full-length Dcsbis protein contains an N-terminal GAF domain and a C-terminal GGDEF domain
-
additional information
-
the GGDEF domain of SadC has a typical GGDEF structure and the alpha-helix connecting the transmembrane domains with SadC GGDEF domain is essential for SadC to form DGC oligomers. Membrane association of SadC promotes its DGC activity by affecting the formation of active DGC oligomers. The alpha-helix of amino acid residues 300-322 is necessary for SadC300-487 to form active hexamers, hexameric and monomeric structures. The structure of SadC323-487 contains five beta-sheets sandwiched by five alpha-helices, which is a typical GGDEF structure. Enzyme mutants structure-function analysis, overview
-
additional information
-
the GGDEF domain of SadC has a typical GGDEF structure and the alpha-helix connecting the transmembrane domains with SadC GGDEF domain is essential for SadC to form DGC oligomers. Membrane association of SadC promotes its DGC activity by affecting the formation of active DGC oligomers. The alpha-helix of amino acid residues 300-322 is necessary for SadC300-487 to form active hexamers, hexameric and monomeric structures. The structure of SadC323-487 contains five beta-sheets sandwiched by five alpha-helices, which is a typical GGDEF structure. Enzyme mutants structure-function analysis, overview
-
additional information
-
the GGDEF domain of SadC has a typical GGDEF structure and the alpha-helix connecting the transmembrane domains with SadC GGDEF domain is essential for SadC to form DGC oligomers. Membrane association of SadC promotes its DGC activity by affecting the formation of active DGC oligomers. The alpha-helix of amino acid residues 300-322 is necessary for SadC300-487 to form active hexamers, hexameric and monomeric structures. The structure of SadC323-487 contains five beta-sheets sandwiched by five alpha-helices, which is a typical GGDEF structure. Enzyme mutants structure-function analysis, overview
-
additional information
-
the GGDEF domain of SadC has a typical GGDEF structure and the alpha-helix connecting the transmembrane domains with SadC GGDEF domain is essential for SadC to form DGC oligomers. Membrane association of SadC promotes its DGC activity by affecting the formation of active DGC oligomers. The alpha-helix of amino acid residues 300-322 is necessary for SadC300-487 to form active hexamers, hexameric and monomeric structures. The structure of SadC323-487 contains five beta-sheets sandwiched by five alpha-helices, which is a typical GGDEF structure. Enzyme mutants structure-function analysis, overview
-
additional information
-
compact and elongated dimeric conformation correspond to catalytically active and inactive state, respectively
additional information
-
compact and elongated dimeric conformation correspond to catalytically active and inactive state, respectively
-
additional information
-
compact and elongated dimeric conformation correspond to catalytically active and inactive state, respectively
additional information
-
enzyme GcsA consists of two per-ARNT-sim (PAS) domains, followed by a canonical conserved central sequence pattern (GGDEF) domain and a truncated EAL domain
additional information
enzyme GcsA consists of two per-ARNT-sim (PAS) domains, followed by a canonical conserved central sequence pattern (GGDEF) domain and a truncated EAL domain
additional information
-
enzyme GcsA consists of two per-ARNT-sim (PAS) domains, followed by a canonical conserved central sequence pattern (GGDEF) domain and a truncated EAL domain
-
additional information
-
enzyme GcsA consists of two per-ARNT-sim (PAS) domains, followed by a canonical conserved central sequence pattern (GGDEF) domain and a truncated EAL domain
-
additional information
-
compact and elongated dimeric conformation correspond to catalytically active and inactive state, respectively
-
additional information
-
enzyme GcsA consists of two per-ARNT-sim (PAS) domains, followed by a canonical conserved central sequence pattern (GGDEF) domain and a truncated EAL domain
-
additional information
-
compact and elongated dimeric conformation correspond to catalytically active and inactive state, respectively
additional information
-
compact and elongated dimeric conformation correspond to catalytically active and inactive state, respectively
-
additional information
-
the GGDEF domain is responsible for the diguanylate cyclase activity
additional information
the periplasmic portion of CdgH forms a type I homodimer in solution which undergoes conformational changes upon L-arginine binding. The dimerization mode requires both tandem PBPb domains. Homodimerization leads to alignment of the two GGDEF domains, resulting in 2fold symmetry that enables the enzyme to catalyze c-diGMP synthesis
additional information
-
the periplasmic portion of CdgH forms a type I homodimer in solution which undergoes conformational changes upon L-arginine binding. The dimerization mode requires both tandem PBPb domains. Homodimerization leads to alignment of the two GGDEF domains, resulting in 2fold symmetry that enables the enzyme to catalyze c-diGMP synthesis
-
additional information
-
the periplasmic portion of CdgH forms a type I homodimer in solution which undergoes conformational changes upon L-arginine binding. The dimerization mode requires both tandem PBPb domains. Homodimerization leads to alignment of the two GGDEF domains, resulting in 2fold symmetry that enables the enzyme to catalyze c-diGMP synthesis
-
additional information
-
the HD-GYP phosphodiesterase domain of RpfG, which is part of a system necessary for the diffusible signalling factor dependent production of extracellular pathogenicity, interacts directly with diguanylate cyclase GGDEF domain-containing proteins. Physical linkage between quorum-sensing and cyclic diguanylate signalling pathways
additional information
Q8PPS5
at micromolar concentrations, the protein exists predominantly as a dimeric species
additional information
-
at micromolar concentrations, the protein exists predominantly as a dimeric species
additional information
DgcA contains an intact GGDEF domain that functions as an active diguanylate cyclase
additional information
-
DgcA contains an intact GGDEF domain that functions as an active diguanylate cyclase
additional information
-
DgcA contains an intact GGDEF domain that functions as an active diguanylate cyclase
-
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
additional information
phosphoprotein
enzyme is activated by phosphorylation of residue D53. In vitro, enzyme PleD can be activated by beryllium fluoride, resulting in dimerization and synthesis of cyclic diguanylate
phosphoprotein
-
localization of response regulator PleD to the stalked pole requires its activation by phosphorylation and is dependent on the polar kinases DivJ and PleC
phosphoprotein
when activated by phosphorylation, yellow fluorescent protein (YFP)-tagged WspR forms clusters that are visible in individual cells by fluorescence microscopy. Unphosphorylated WspR is diffuse in cells and not visible. In general, increased cluster formation correlates with increased in vivo and in vitro diguanylate cyclase activities of variants. In addition, WspR specific activity is strongly concentration dependent in vitro, and the effect of the protein concentration on diguanylate cyclase activity is magnified when WspR is treated with the phosphor analog beryllium fluoride. Cluster formation appears to be an intrinsic property of phosphorylated WspR
additional information
-
pseudo-phosphorylation by beryllium fluoride (BeF3-) modification at residue Asp53 in Rec-domain (D1), tightens dimer
additional information
pseudo-phosphorylation by beryllium fluoride (BeF3-) modification at residue Asp53 in Rec-domain (D1), tightens dimer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
after activation by berillium trifluoride. Activation causes rearrangement of an adaptor domain which in turn promotes dimer formation. The substrate analogue GTPgammaS and two putative cations are bound to the active sites. Identification of a second cyclic diguanylate binding mode that crosslinks the diguanylate cyclase domains within a protein dimer and results in noncompetitive product inhibition
BeF3-/Mg2+-modified PleD (100 microM) in presence of cyclic di-3,5-guanylate (0.2 mM) and substrate-analog GTPalphaS (1 mM), hanging-drop vapour-diffusion: equal volumes protein solution (10 mg/ml) and precipitant solution (0.1M HEPES pH 8, 0.73 M Na2SO4), crystals: needle shape, space group: P2(1)2(1)2(1), unit cell parameters: a: 128.9, b: 132.6, c: 88.4, resolved by molecular replacement using PDB: 1W25 as model, tightened dimer interface at the dyad symmetric stem between D1/D2 domains of the two monomers upon rotation of D2 relative to D1, restructured beta4alpha4 loop compared to nonactivated state, GTPalphaS bound to both diguanylate cyclase (GGDEF) domain active sites, 2fold symmetric crosslinking of GGDEF domains of the structural dimer in presence of cyclic di-3,5-guanylate, cyclic di-3,5-guanylate bound to allosteric (inhibitory) site similarly to nonactivated state
in complex with product cyclic diguanylate. The guanine base is H-bonded to N335 and D344, whereas the ribosyl and alpha-phosphate moieties extend over the beta2-beta3-hairpin that carries the GGEEF signature motif. In the crystal, cyclic diguanylate molecules are crosslinking active sites of adjacent dimers. In solution, two diguanylate cyclase doamins of a dimer may align in a twofold symmetric way to catalyze synthesis of cyclic diguanylate
-
structural characterization of the oxygen-sensing globin domain, the middle domain and the catalytic GGDEF omain in apo and substrate-bound forms. The structural changes between the iron(III) and iron(II) forms of the sensor globin domain suggest a mechanism for oxygen-dependent regulation. Enzyme forms a constitutive dimer and in this form its enzymatic activity is regulated by oxygen binding. The middle domain of DosC connects the sensory and effector modules and is likely to be both essential for and directly involved in the intramolecular signal transduction in DosC
the zinc ion is bound to the 3His/1Cys motif of the regulatory chemoreceptor zinc-binding domain, which mediates subunit contact within the dimeric enzyme
purified Lcd1GAF domain in complex with cAMP, sitting drop method, mixing 0.0015 ml of 8 mg/ml protein with 4 mM of cAMP and 0.0015 ml of 0.2 M sodium citrate and 20% w/v PEG 3350, 2-4 weeks at 18°C, X-ray diffraction structure determination and analysis at 2.15 A resolution, modelling
the crystal structure of G-A1U3W3 (residues 155-312) is determined at 1.83 A resolution using the selenomethionyl SAD method. Co-crystallization with GTP results in enzymatic synthesis of c-di-GMP
in complex with cyclic di-3',5'-guanylate (PDB: 3BRE), solved by molecular replacement using PDB: 1W25 as model, tetramer of two anti-parallel dimers with physically blocked active site, hanging-drop vapour-diffusion: equal volumes protein solution (5-30 mg/ml) and reservoir solution (0.1 M Tris-HCl pH 8, 2.9 M NaCl, 15% xylitol), crystal: space group: C2, unit cell parameter: a: 144.5, b: 72.8, c: 106.1, beta: 110.8, asymmetric unit: two molecules with active site facing each other and four molecules cyclic di-3',5'-guanylate bound to residues Arg242 and Arg198 and two Mg2+ ions, resemblance of GAF domain assembly
-
purified recombinant truncated enzymes SadC323-487 and SadC300-487, X-ray diffraction structure determination and analysis at 1.8 A and 2.8 A resolution, respectively. The structure contains ine Mg2+, molecular replacement structure analysis
to 2.9 A resolution. A peptide loop extending from the GAF domain occupies the conserved inhibition site, thereby largely relieving the product-inhibition effect. A large hydrophobic pocket is observed in the GAF domain
GcbC bound to c-di-GMP, X-ray diffraction structure determination and analysis
isoform GcbC physically interacting with its target protein at a conserved interface, and this interface can be predictive of diguanylate cyclase-target protein interactions. Physical interaction is necessary for the enzyme to maximally signal its target
the crystal structure of full-length WspR is determined at 2.8 A resolution, of WspGCN4-RGGDEF at 1.94 A resolution
-
structures of an active-like dimeric conformation with both active sites facing each other, of an inactive dimeric conformation, locked by cyclic di-GMP bound at the inhibitory site, and of a single mutant with the R158A mutation at the inhibitory site. A comparison with structurally characterized DGC homologues from mesophiles reveals the presence of a higher number of salt bridges in the hyperthermophile enzyme
purified recombinant periplasmic portion (residues 46-491, which includes the tandem PBPb-I and PBPb-II domains) of C-terminally His6-tagged CdgH, X-ray diffraction structure determination and analysis at 2.6 A resolution
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K226A
site-directed mutagenesis, biofilm formation of the mutant is inhibited
S68A
site-directed mutagenesis, biofilm formation of the mutant is inhibited
Y43A
site-directed mutagenesis, biofilm formation of the mutant is partially inhibited, and cell motility is inhibited
S68A
-
site-directed mutagenesis, biofilm formation of the mutant is inhibited
-
Y43A
-
site-directed mutagenesis, biofilm formation of the mutant is partially inhibited, and cell motility is inhibited
-
S68A
-
site-directed mutagenesis, biofilm formation of the mutant is inhibited
-
Y43A
-
site-directed mutagenesis, biofilm formation of the mutant is partially inhibited, and cell motility is inhibited
-
S68A
-
site-directed mutagenesis, biofilm formation of the mutant is inhibited
-
Y43A
-
site-directed mutagenesis, biofilm formation of the mutant is partially inhibited, and cell motility is inhibited
-
D53N
DELTAR359/DELTAD362
mutations in allosteric binding site of cyclic diguanylate, abolish cyclic diguanylate binding, strong decrease in catalytic activity
E370Q
EE370GG
mutation in active site, complete loss of catalytic activity without effect on allosteric binding of cyclic diguanylate
R148A
increase in allosteric binding of cyclic diguanylate and increase in catalytic activity
R148A/R178A
R148A/R178A/R313A
triple mutant, KD for binding of cyclic di-3,5-guanylate: 4 microM (10fold higher than wild-type), 60fold increased KI for product inhibition by cyclic di-3,5-guanylate, residual catalytic activity
R178A
increase in allosteric binding of cyclic diguanylate and increase in catalytic activity
R359A
mutation in allosteric binding site of cyclic diguanylate, strong decrease in cyclic diguanylate binding, strong decrease in catalytic activity
R390A
mutation in allosteric binding site of cyclic diguanylate, strong decrease in cyclic diguanylate binding. Catalytic activity comaprable to wild-type
Y26A
D418A
A68T
site-directed mutagenesis, the mutant cell motility and biofilm formation are partially inhibited
D333A
site-directed mutagenesis, biofilm formation of the mutant is inhibited
D342A
site-directed mutagenesis, biofilm formation of the mutant is inhibited
D350A
site-directed mutagenesis, biofilm formation of the mutant is inhibited
D368A
site-directed mutagenesis, biofilm formation of the mutant is inhibited
D368K
site-directed mutagenesis, biofilm formation of the mutant is inhibited
D376A
site-directed mutagenesis, biofilm formation of the mutant is inhibited
E377A
site-directed mutagenesis, biofilm formation of the mutant is inhibited
F337A
site-directed mutagenesis, biofilm formation of the mutant is inhibited
F378A
site-directed mutagenesis, biofilm formation of the mutant is inhibited
G374A
site-directed mutagenesis, biofilm formation of the mutant is inhibited
G375A
site-directed mutagenesis, biofilm formation of the mutant is inhibited
H223A
site-directed mutagenesis, biofilm formation of the mutant is inhibited
H79L/H83L
site-directed mutagenesis, the mutant shows increased activity compared to wild-type enzyme, cellular localization is unaltered
H79L/H83L/E208Q
site-directed mutagenesis, inactive mutant, cellular localization is unaltered
H93A
site-directed mutagenesis, the mutant has no heme and is inactive
K224A
site-directed mutagenesis, biofilm formation of the mutant is inhibited
K338A
site-directed mutagenesis, the mutant cell motility and biofilm formation are partially inhibited
L300A
site-directed mutagenesis, the mutant biofilm formation is partially inhibited
L300D
site-directed mutagenesis, the mutant cell motility is inhibited, biofilm formation of the mutant is inhibited
L353A
site-directed mutagenesis, biofilm formation of the mutant is inhibited
L353D
site-directed mutagenesis, the mutant cell motility is inhibited, and biofilm formation of the mutant is inhibited
L65G
site-directed mutagenesis, heme distal amino acid replacement leading to reduced activity compared to wild-type
L65Q
site-directed mutagenesis, heme distal amino acid replacement leading to reduced activity compared to wild-type
N341A
site-directed mutagenesis, biofilm formation of the mutant is inhibited
R306A
site-directed mutagenesis, biofilm formation of the mutant is inhibited
R372A
site-directed mutagenesis, the mutant cell motility is inhibited, and biofilm formation of the mutant is inhibited
Y43A
D70A
mutated in the response regulator domain, no significant formation of clusters
E253A
mutated in active site, protein forms subcellular clusters in broth-grown cells
GGAAF
-
catalytically dead mutant of active site motif GGEEF, inactive, able to bind cyclic di-3,5-guanylate although nucleotide-free when purified, compact dimer-tetramer equilibrium like nucleotide-free wild-type
L167D
L170D
R198A
R242A
R595A
site-directed mutagenesis, the mutant shows similar activity compared to wild-type enzyme
R641A/R644A
site-directed mutagenesis, the mutant shows similar activity compared to wild-type enzyme
R672A
site-directed mutagenesis, the mutant shows increased activity compared to wild-type enzyme
V72D
mutated in the response regulator domain, no significant formation of clusters
R595A
-
site-directed mutagenesis, the mutant shows similar activity compared to wild-type enzyme
-
R595A
-
site-directed mutagenesis, the mutant shows similar activity compared to wild-type enzyme
-
R595A
-
site-directed mutagenesis, the mutant shows similar activity compared to wild-type enzyme
-
R595A
-
site-directed mutagenesis, the mutant shows similar activity compared to wild-type enzyme
-
R595A
-
site-directed mutagenesis, the mutant shows similar activity compared to wild-type enzyme
-
R595A
-
site-directed mutagenesis, the mutant shows similar activity compared to wild-type enzyme
-
R595A
-
site-directed mutagenesis, the mutant shows similar activity compared to wild-type enzyme
-
D413K
site-directed mutagenesis, the mutant shows slightly reduced activity compared to wild-type
E360R
site-directed mutagenesis, the mutant shows about 50% increased activity compared to wild-type, but reduced biofilm formation despite elevated levels of c-di-GMP production
E429R
site-directed mutagenesis, the mutant shows slightly increased activity compared to wild-type, but reduced biofilm formation despite elevated levels of c-di-GMP production
R363E
site-directed mutagenesis, the I-site mutant shows a 20fold increase in c-di-GMP production
R366E
site-directed mutagenesis, the I-site mutant shows a 16fold increase in c-di-GMP production
D413K
Pseudomonas fluorescens Pfl01
-
site-directed mutagenesis, the mutant shows slightly reduced activity compared to wild-type
-
E360R
Pseudomonas fluorescens Pfl01
-
site-directed mutagenesis, the mutant shows about 50% increased activity compared to wild-type, but reduced biofilm formation despite elevated levels of c-di-GMP production
-
E429R
Pseudomonas fluorescens Pfl01
-
site-directed mutagenesis, the mutant shows slightly increased activity compared to wild-type, but reduced biofilm formation despite elevated levels of c-di-GMP production
-
R366E
Pseudomonas fluorescens Pfl01
-
site-directed mutagenesis, the I-site mutant shows a 16fold increase in c-di-GMP production
-
WspGCN4-RGGDEF
-
fusion protein, coiled-coil segment of GCN4 from Saccharomyces cerevisiae, C-terminal diguanylate cyclase domain with the characteristic GGDEF motif and the active site
WspRD70N
-
mutant, point mutation at the predicted phosphorylation site in the REC domain
WspRGGDEF
-
residues 172-347, C-terminal diguanylate cyclase domain with the characteristic GGDEF motif and the active site
WspRstalk-GGDEF
-
residues 140-347, catalytic activity is modulated by the helical stalk motif, C-terminal diguanylate cyclase domain with the characteristic GGDEF motif and the active site
D177A
mutation in salt bridge, decrease in melting temperature by 12.3 degrees
E196A
mutation in salt bridge, decrease in melting temperature by 4.2 degrees
R158A
R233A
mutation in salt bridge, decrease in melting temperature by 8.6 degrees
D177A
-
mutation in salt bridge, decrease in melting temperature by 12.3 degrees
-
E196A
-
mutation in salt bridge, decrease in melting temperature by 4.2 degrees
-
R158A
-
mutation at the inhibitory site, abolishing product inhibition and unproductive dimerization
-
R233A
-
mutation in salt bridge, decrease in melting temperature by 8.6 degrees
-
D484E
RXXD allosteric inhibition site of the protein is mutated (VC2370(142)-D484E) because it is shown, using HPLC-MS-MS, that c-di-GMP copurifies with native VC2370. Mutation of this RXXD site prevents c-di-GMP copurification. Also, mutation of the site ensures that c-di-GMP produced during the in vitro reaction is not able to inhibit enzyme activity
K759A
Q8PPS5
mutagenesis of a conserved lysine residue, results in a severe reduction in dihuanylate cyclase activity, kcat value is almost 100fold lower than that of the wild-type protein while the K1 and K2 values do not change very much
additional information
E370Q
mutation in active site, complete loss of catalytic activity without effect on allosteric binding of cyclic diguanylate
E370Q
mainly dimeric, inactive mutant of the guanylate cyclase domain GG(D/E)EF (Mg2+ coordination), no activation by BeF3 or protein concentration above 50 microM
R148A/R178A
increase in allosteric binding of cyclic diguanylate and increase in catalytic activity
D418A
-
site-directed mutagenesis, replacing the essential aspartic acid residue with alanine (SGAEF), resulting in a mutant that is not defective for growth when compared with the wild-type strain, but the enzyme is catalytically inactive and shows abolished negative Pel regulation, instead the mutation of the GcpA A-site enhances the production of Pel
D418A
-
site-directed mutagenesis, replacing the essential aspartic acid residue with alanine (SGAEF), resulting in a mutant that is not defective for growth when compared with the wild-type strain, but the enzyme is catalytically inactive and shows abolished negative Pel regulation, instead the mutation of the GcpA A-site enhances the production of Pel
-
Y43A
site-directed mutagenesis, heme distal amino acid replacement leading to reduced activity compared to wild-type
L167D
-
predominantly monomeric, weakly associated dimer, purifies cyclic di-3,5-guanylate-bound, inactive (also upon cyclic di-3,5-guanylate hydrolysis)
L170D
-
highly active also in cyclic di-3,5-guanylate-bound state, in compact dimer-tetramer equilibrium like nucleotide-free wild-type
L170D
mutated in linker stalk, protein forms subcellular clusters in broth-grown cells
R198A
-
mutant of side chain complementing the inhibitory site R242xxD, highly active, low cyclic di-3,5-guanylate affinity, nucleotide-free, in compact dimer-tetramer equilibrium like nucleotide-free wild-type
R198A
mutated in I site, protein forms subcellular clusters in broth-grown cells
R242A
-
mutant of inhibitory site RxxD, highly active, low cyclic di-3,5-guanylate affinity, nucleotide-free, in compact dimer-tetramer equilibrium like nucleotide-free wild-type
R242A
-
mutant sows activity and is used as a target enzyme. Mutation locks the enzyme in a constitutively active state
R158A
mutation of a key residue in the putative regulatory I-site, product inhibition is substantially alleviated
R158A
-
mutant shows increased enzymatic activity compared to wild-type, mutant shows 4fold lower expression level compared to wild-type which might be due to higher enzymatic activity of mutant R158A and its increased toxicity for cells
R158A
mutation at the inhibitory site, abolishing product inhibition and unproductive dimerization
additional information
-
enzyme disruption mutants of MifA or MifB show increased flagellin levels, while mutlicopy expression decreases them
additional information
generation of truncated enzyme mutants BpeGReg1-155, BpeGReg1-266, BpeGReg1-296, BpeGReg156-475, BpeGReg267-475, and BpeGReg297-475
additional information
-
generation of truncated enzyme mutants BpeGReg1-155, BpeGReg1-266, BpeGReg1-296, BpeGReg156-475, BpeGReg267-475, and BpeGReg297-475
additional information
-
generation of truncated enzyme mutants BpeGReg1-155, BpeGReg1-266, BpeGReg1-296, BpeGReg156-475, BpeGReg267-475, and BpeGReg297-475
-
additional information
-
generation of truncated enzyme mutants BpeGReg1-155, BpeGReg1-266, BpeGReg1-296, BpeGReg156-475, BpeGReg267-475, and BpeGReg297-475
-
additional information
-
generation of truncated enzyme mutants BpeGReg1-155, BpeGReg1-266, BpeGReg1-296, BpeGReg156-475, BpeGReg267-475, and BpeGReg297-475
-
additional information
-
cells overexpressing diguanylate cyclase YddV display an abnormal cell division process when high levels of cyclic diguanylate are present. Gene yvvD is co-transcribed with dos, a heme based oxygen sensor with cyclic diguanylate phosphodiesterase activity
additional information
-
a mutant, carrying an adrA mutation resulting in GGDEF -> GGAAF change in AdrA protein catalytic site, is constructed
additional information
chromosomal replacement of the corresponding wild-type gene by mVENUS fusions to dgcZ wild-type or mutant variants, as well as by mCHERRY fusions to frdA and frdB, are achieved by standardFRED-mediated recombineering. In each case, the PRham-ccdB-kan element replaced the wild-type locus in the precursor strain. The dgcZ(+) and frdA(+) control strains are obtained by replacing the PRham-ccdBkan element with the dgcZ and frdA genes amplified from Escherichia coli strain MG1655
additional information
-
chromosomal replacement of the corresponding wild-type gene by mVENUS fusions to dgcZ wild-type or mutant variants, as well as by mCHERRY fusions to frdA and frdB, are achieved by standardFRED-mediated recombineering. In each case, the PRham-ccdB-kan element replaced the wild-type locus in the precursor strain. The dgcZ(+) and frdA(+) control strains are obtained by replacing the PRham-ccdBkan element with the dgcZ and frdA genes amplified from Escherichia coli strain MG1655
additional information
-
disruption of dgc genes markedly reduces in vivo cellulose production in Acetobacter xylinum
additional information
isolated G-A1U3W3 domain (residues 155312) has full enzymatic activity and synthesize c-di-GMP
additional information
-
deletion of gene PA4367 results in severe defect in swarming motility and a hyperbiofilm phenotype. Mutant exhibits increased cellular pools of cyclic di-3,5-guanylate, increased synthesis of a polysaccharide produced by the pel locus and decreased flagellar reversals. GGDQF and EAL domains of BifA are both required for complementation of the mutant
additional information
mutating the critical GGEEF motif to GGAAF results in loss of stimulation of Pel polysaccharide production and biofilm formation
additional information
mutating the critical GGEEF motif to GGAAF results in loss of stimulation of Pel polysaccharide production and biofilm formation
additional information
-
mutating the critical GGEEF motif to GGAAF results in loss of stimulation of Pel polysaccharide production and biofilm formation
additional information
generation of a catalytically inactive HsbD GGAAF mutant which does not trigger the intracellular c-di-GMP output. Engineering of hsbD deletion in the Pseudomonas aeruginosa wild-type and DELTAhptB (hptB deletion) background, phenotypes, overview. In the DELTAhptBDELTAhsbD background, both c-di-GMP levels and the expression of the cdrA-gfp fusion are reduced when compared to the DELTAhptB background and they are similar to the wild-type strain. Differences in c-di-GMP levels or in the expression of the reporter construct between a DELTAhsbD mutant and the wild-type strain are not observed
additional information
-
generation of a catalytically inactive HsbD GGAAF mutant which does not trigger the intracellular c-di-GMP output. Engineering of hsbD deletion in the Pseudomonas aeruginosa wild-type and DELTAhptB (hptB deletion) background, phenotypes, overview. In the DELTAhptBDELTAhsbD background, both c-di-GMP levels and the expression of the cdrA-gfp fusion are reduced when compared to the DELTAhptB background and they are similar to the wild-type strain. Differences in c-di-GMP levels or in the expression of the reporter construct between a DELTAhsbD mutant and the wild-type strain are not observed
additional information
construction of DELTAPPA3177 deletion strain, phenotype, overview
additional information
-
construction of DELTAPPA3177 deletion strain, phenotype, overview
additional information
construction of an N-terminally truncated SadC containing amino acid residue 300-487, which included the entire GGDEF domain and 23 amino acid residues at the N-terminus to link GGDEF domain with the transmembrane domains. Recombinant strain PAO1/pSadC300-487 fails to promote bacterial cell aggregation even if its expression is induced by 2% arabinose. Moreover, SadC300-487 does not significantly enhance the biofilm formation of PAO1 although SadC300-487 can increase Psl production to a level close to the full-length SadC when induced by 2% arabinose. The crystal structure of SadC323-487 indicates that this truncated SadC is a monomer in the asymmetric unit. The structure of SadC323-487 contains five beta-sheets sandwiched by five alpha-helices, which is a typical GGDEF structure. SadC300-487 can catalyze the synthesis of c-di-GMP in vitro, but SadC323-487 cannot, structure-function analysis, overview
additional information
-
construction of an N-terminally truncated SadC containing amino acid residue 300-487, which included the entire GGDEF domain and 23 amino acid residues at the N-terminus to link GGDEF domain with the transmembrane domains. Recombinant strain PAO1/pSadC300-487 fails to promote bacterial cell aggregation even if its expression is induced by 2% arabinose. Moreover, SadC300-487 does not significantly enhance the biofilm formation of PAO1 although SadC300-487 can increase Psl production to a level close to the full-length SadC when induced by 2% arabinose. The crystal structure of SadC323-487 indicates that this truncated SadC is a monomer in the asymmetric unit. The structure of SadC323-487 contains five beta-sheets sandwiched by five alpha-helices, which is a typical GGDEF structure. SadC300-487 can catalyze the synthesis of c-di-GMP in vitro, but SadC323-487 cannot, structure-function analysis, overview
additional information
construction and expression of the PA0847 transposon mutants DELTAPA0847-1 and DELTAPA0847-2 in Pseudomonas aeruginosa strain PAO1, comparison to wild-type, phenotypes, overview. Generation of an enzyme deletion mutant, DELTAPA0847
additional information
-
construction of DELTAPPA3177 deletion strain, phenotype, overview
-
additional information
-
construction of an N-terminally truncated SadC containing amino acid residue 300-487, which included the entire GGDEF domain and 23 amino acid residues at the N-terminus to link GGDEF domain with the transmembrane domains. Recombinant strain PAO1/pSadC300-487 fails to promote bacterial cell aggregation even if its expression is induced by 2% arabinose. Moreover, SadC300-487 does not significantly enhance the biofilm formation of PAO1 although SadC300-487 can increase Psl production to a level close to the full-length SadC when induced by 2% arabinose. The crystal structure of SadC323-487 indicates that this truncated SadC is a monomer in the asymmetric unit. The structure of SadC323-487 contains five beta-sheets sandwiched by five alpha-helices, which is a typical GGDEF structure. SadC300-487 can catalyze the synthesis of c-di-GMP in vitro, but SadC323-487 cannot, structure-function analysis, overview
-
additional information
-
construction and expression of the PA0847 transposon mutants DELTAPA0847-1 and DELTAPA0847-2 in Pseudomonas aeruginosa strain PAO1, comparison to wild-type, phenotypes, overview. Generation of an enzyme deletion mutant, DELTAPA0847
-
additional information
-
generation of a catalytically inactive HsbD GGAAF mutant which does not trigger the intracellular c-di-GMP output. Engineering of hsbD deletion in the Pseudomonas aeruginosa wild-type and DELTAhptB (hptB deletion) background, phenotypes, overview. In the DELTAhptBDELTAhsbD background, both c-di-GMP levels and the expression of the cdrA-gfp fusion are reduced when compared to the DELTAhptB background and they are similar to the wild-type strain. Differences in c-di-GMP levels or in the expression of the reporter construct between a DELTAhsbD mutant and the wild-type strain are not observed
-
additional information
-
construction of DELTAPPA3177 deletion strain, phenotype, overview
-
additional information
-
construction of an N-terminally truncated SadC containing amino acid residue 300-487, which included the entire GGDEF domain and 23 amino acid residues at the N-terminus to link GGDEF domain with the transmembrane domains. Recombinant strain PAO1/pSadC300-487 fails to promote bacterial cell aggregation even if its expression is induced by 2% arabinose. Moreover, SadC300-487 does not significantly enhance the biofilm formation of PAO1 although SadC300-487 can increase Psl production to a level close to the full-length SadC when induced by 2% arabinose. The crystal structure of SadC323-487 indicates that this truncated SadC is a monomer in the asymmetric unit. The structure of SadC323-487 contains five beta-sheets sandwiched by five alpha-helices, which is a typical GGDEF structure. SadC300-487 can catalyze the synthesis of c-di-GMP in vitro, but SadC323-487 cannot, structure-function analysis, overview
-
additional information
-
construction and expression of the PA0847 transposon mutants DELTAPA0847-1 and DELTAPA0847-2 in Pseudomonas aeruginosa strain PAO1, comparison to wild-type, phenotypes, overview. Generation of an enzyme deletion mutant, DELTAPA0847
-
additional information
-
construction of DELTAPPA3177 deletion strain, phenotype, overview
-
additional information
-
construction of an N-terminally truncated SadC containing amino acid residue 300-487, which included the entire GGDEF domain and 23 amino acid residues at the N-terminus to link GGDEF domain with the transmembrane domains. Recombinant strain PAO1/pSadC300-487 fails to promote bacterial cell aggregation even if its expression is induced by 2% arabinose. Moreover, SadC300-487 does not significantly enhance the biofilm formation of PAO1 although SadC300-487 can increase Psl production to a level close to the full-length SadC when induced by 2% arabinose. The crystal structure of SadC323-487 indicates that this truncated SadC is a monomer in the asymmetric unit. The structure of SadC323-487 contains five beta-sheets sandwiched by five alpha-helices, which is a typical GGDEF structure. SadC300-487 can catalyze the synthesis of c-di-GMP in vitro, but SadC323-487 cannot, structure-function analysis, overview
-
additional information
-
construction and expression of the PA0847 transposon mutants DELTAPA0847-1 and DELTAPA0847-2 in Pseudomonas aeruginosa strain PAO1, comparison to wild-type, phenotypes, overview. Generation of an enzyme deletion mutant, DELTAPA0847
-
additional information
-
construction of DELTAPPA3177 deletion strain, phenotype, overview
-
additional information
-
construction of an N-terminally truncated SadC containing amino acid residue 300-487, which included the entire GGDEF domain and 23 amino acid residues at the N-terminus to link GGDEF domain with the transmembrane domains. Recombinant strain PAO1/pSadC300-487 fails to promote bacterial cell aggregation even if its expression is induced by 2% arabinose. Moreover, SadC300-487 does not significantly enhance the biofilm formation of PAO1 although SadC300-487 can increase Psl production to a level close to the full-length SadC when induced by 2% arabinose. The crystal structure of SadC323-487 indicates that this truncated SadC is a monomer in the asymmetric unit. The structure of SadC323-487 contains five beta-sheets sandwiched by five alpha-helices, which is a typical GGDEF structure. SadC300-487 can catalyze the synthesis of c-di-GMP in vitro, but SadC323-487 cannot, structure-function analysis, overview
-
additional information
-
construction and expression of the PA0847 transposon mutants DELTAPA0847-1 and DELTAPA0847-2 in Pseudomonas aeruginosa strain PAO1, comparison to wild-type, phenotypes, overview. Generation of an enzyme deletion mutant, DELTAPA0847
-
additional information
-
construction of DELTAPPA3177 deletion strain, phenotype, overview
-
additional information
-
construction of an N-terminally truncated SadC containing amino acid residue 300-487, which included the entire GGDEF domain and 23 amino acid residues at the N-terminus to link GGDEF domain with the transmembrane domains. Recombinant strain PAO1/pSadC300-487 fails to promote bacterial cell aggregation even if its expression is induced by 2% arabinose. Moreover, SadC300-487 does not significantly enhance the biofilm formation of PAO1 although SadC300-487 can increase Psl production to a level close to the full-length SadC when induced by 2% arabinose. The crystal structure of SadC323-487 indicates that this truncated SadC is a monomer in the asymmetric unit. The structure of SadC323-487 contains five beta-sheets sandwiched by five alpha-helices, which is a typical GGDEF structure. SadC300-487 can catalyze the synthesis of c-di-GMP in vitro, but SadC323-487 cannot, structure-function analysis, overview
-
additional information
-
construction and expression of the PA0847 transposon mutants DELTAPA0847-1 and DELTAPA0847-2 in Pseudomonas aeruginosa strain PAO1, comparison to wild-type, phenotypes, overview. Generation of an enzyme deletion mutant, DELTAPA0847
-
additional information
-
construction of DELTAPPA3177 deletion strain, phenotype, overview
-
additional information
-
construction of an N-terminally truncated SadC containing amino acid residue 300-487, which included the entire GGDEF domain and 23 amino acid residues at the N-terminus to link GGDEF domain with the transmembrane domains. Recombinant strain PAO1/pSadC300-487 fails to promote bacterial cell aggregation even if its expression is induced by 2% arabinose. Moreover, SadC300-487 does not significantly enhance the biofilm formation of PAO1 although SadC300-487 can increase Psl production to a level close to the full-length SadC when induced by 2% arabinose. The crystal structure of SadC323-487 indicates that this truncated SadC is a monomer in the asymmetric unit. The structure of SadC323-487 contains five beta-sheets sandwiched by five alpha-helices, which is a typical GGDEF structure. SadC300-487 can catalyze the synthesis of c-di-GMP in vitro, but SadC323-487 cannot, structure-function analysis, overview
-
additional information
-
construction and expression of the PA0847 transposon mutants DELTAPA0847-1 and DELTAPA0847-2 in Pseudomonas aeruginosa strain PAO1, comparison to wild-type, phenotypes, overview. Generation of an enzyme deletion mutant, DELTAPA0847
-
additional information
-
construction of DELTAPPA3177 deletion strain, phenotype, overview
-
additional information
-
construction of an N-terminally truncated SadC containing amino acid residue 300-487, which included the entire GGDEF domain and 23 amino acid residues at the N-terminus to link GGDEF domain with the transmembrane domains. Recombinant strain PAO1/pSadC300-487 fails to promote bacterial cell aggregation even if its expression is induced by 2% arabinose. Moreover, SadC300-487 does not significantly enhance the biofilm formation of PAO1 although SadC300-487 can increase Psl production to a level close to the full-length SadC when induced by 2% arabinose. The crystal structure of SadC323-487 indicates that this truncated SadC is a monomer in the asymmetric unit. The structure of SadC323-487 contains five beta-sheets sandwiched by five alpha-helices, which is a typical GGDEF structure. SadC300-487 can catalyze the synthesis of c-di-GMP in vitro, but SadC323-487 cannot, structure-function analysis, overview
-
additional information
-
construction and expression of the PA0847 transposon mutants DELTAPA0847-1 and DELTAPA0847-2 in Pseudomonas aeruginosa strain PAO1, comparison to wild-type, phenotypes, overview. Generation of an enzyme deletion mutant, DELTAPA0847
-
additional information
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mutant bearing a GGDEF-to-GGAAF mutation is not able to complement a deletion mutant
additional information
mutant bearing a GGDEF-to-GGAAF mutation is not able to complement a deletion mutant
additional information
mutant bearing a GGDEF-to-GGAAF mutation is not able to complement a deletion mutant
additional information
-
mutant bearing a GGDEF-to-GGAAF mutation is able to complement a deletion mutant
additional information
mutant bearing a GGDEF-to-GGAAF mutation is able to complement a deletion mutant
additional information
mutant bearing a GGDEF-to-GGAAF mutation is able to complement a deletion mutant
additional information
-
generation of the adrA mutant harbouring the pCdrA::gfpC biosensor vector, the adrA mutant shows enhanced fliC expression
additional information
a mutagenic bacterial two-hybrid (B2H) screen is conducted to identify alleles of GcbC that fail to interact with LapD. Disruption of the I-site of GcbC leads to deregulation of c-di-GMP production
additional information
-
a mutagenic bacterial two-hybrid (B2H) screen is conducted to identify alleles of GcbC that fail to interact with LapD. Disruption of the I-site of GcbC leads to deregulation of c-di-GMP production
additional information
-
generation of the adrA mutant harbouring the pCdrA::gfpC biosensor vector, the adrA mutant shows enhanced fliC expression
-
additional information
Pseudomonas fluorescens Pfl01
-
a mutagenic bacterial two-hybrid (B2H) screen is conducted to identify alleles of GcbC that fail to interact with LapD. Disruption of the I-site of GcbC leads to deregulation of c-di-GMP production
-
additional information
-
mutation in the GGDEF motif from GGDEF to GGAAF abolishes the cyclic diguanylate synthesis ability of GcsA
additional information
mutation in the GGDEF motif from GGDEF to GGAAF abolishes the cyclic diguanylate synthesis ability of GcsA
additional information
-
construction of a gcsA-deletion mutant. The deletion and complementation of gcsA shows no obvious influence on the growth rate of the strains in liquid LB broth. The normalized GFP fluorescence in the gcsA-deletion strain and complemented strain shows no significant difference compared to that in the wild-type strain at 24 h after inoculation. The gcsA deletion mutant contains about a 27% lower amount of c-di-GMP, and the gcsA-complemented strain contains about a 30% higher amount of c-di-GMP compared to the wild-type strain at the 5 h time point. Comparison of swimming motility, biofilm formation, and surface morphology of the gcsA mutant and complemented strain, overview
additional information
construction of a gcsA-deletion mutant. The deletion and complementation of gcsA shows no obvious influence on the growth rate of the strains in liquid LB broth. The normalized GFP fluorescence in the gcsA-deletion strain and complemented strain shows no significant difference compared to that in the wild-type strain at 24 h after inoculation. The gcsA deletion mutant contains about a 27% lower amount of c-di-GMP, and the gcsA-complemented strain contains about a 30% higher amount of c-di-GMP compared to the wild-type strain at the 5 h time point. Comparison of swimming motility, biofilm formation, and surface morphology of the gcsA mutant and complemented strain, overview
additional information
-
construction of a gcsA-deletion mutant. The deletion and complementation of gcsA shows no obvious influence on the growth rate of the strains in liquid LB broth. The normalized GFP fluorescence in the gcsA-deletion strain and complemented strain shows no significant difference compared to that in the wild-type strain at 24 h after inoculation. The gcsA deletion mutant contains about a 27% lower amount of c-di-GMP, and the gcsA-complemented strain contains about a 30% higher amount of c-di-GMP compared to the wild-type strain at the 5 h time point. Comparison of swimming motility, biofilm formation, and surface morphology of the gcsA mutant and complemented strain, overview
-
additional information
-
construction of a gcsA-deletion mutant. The deletion and complementation of gcsA shows no obvious influence on the growth rate of the strains in liquid LB broth. The normalized GFP fluorescence in the gcsA-deletion strain and complemented strain shows no significant difference compared to that in the wild-type strain at 24 h after inoculation. The gcsA deletion mutant contains about a 27% lower amount of c-di-GMP, and the gcsA-complemented strain contains about a 30% higher amount of c-di-GMP compared to the wild-type strain at the 5 h time point. Comparison of swimming motility, biofilm formation, and surface morphology of the gcsA mutant and complemented strain, overview
-
additional information
-
mutation in the GGDEF motif from GGDEF to GGAAF abolishes the cyclic diguanylate synthesis ability of GcsA
-
additional information
-
construction of a gcsA-deletion mutant. The deletion and complementation of gcsA shows no obvious influence on the growth rate of the strains in liquid LB broth. The normalized GFP fluorescence in the gcsA-deletion strain and complemented strain shows no significant difference compared to that in the wild-type strain at 24 h after inoculation. The gcsA deletion mutant contains about a 27% lower amount of c-di-GMP, and the gcsA-complemented strain contains about a 30% higher amount of c-di-GMP compared to the wild-type strain at the 5 h time point. Comparison of swimming motility, biofilm formation, and surface morphology of the gcsA mutant and complemented strain, overview
-
additional information
-
mutating the Chp8 GGDEF motif impairs cyclic di-GMP production and biofilm formation. Inactivation of the Chp8 phosphodiesterase domain also interferes with cyclic di-GMP production despite an unmodified DGC domain
additional information
-
mutating the Chp8 GGDEF motif impairs cyclic di-GMP production and biofilm formation. Inactivation of the Chp8 phosphodiesterase domain also interferes with cyclic di-GMP production despite an unmodified DGC domain
-
additional information
generation of knockout DELTAslr1143 mutants of Cph2. Whereas wild-type cells are non-motile under high-intensity red light of 640 nm, the mutant DELTAslr1143 displays positive phototaxis. This phenotype can be complemented by overexpression of full-length Slr1143, which also results in an increased cellular c-di-GMP concentration. However, the non-motile phenotype of wild-type cells under high-intensity red light appears not to be due to an elevated cellular c-di-GMP content
additional information
ITC analysis of interactions between different amino acids and the periplasmic portion of CdgH with different truncations and mutants, overview
additional information
-
ITC analysis of interactions between different amino acids and the periplasmic portion of CdgH with different truncations and mutants, overview
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additional information
-
ITC analysis of interactions between different amino acids and the periplasmic portion of CdgH with different truncations and mutants, overview
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
52
Tm of apo-Lcd1GAF domain and of c-di-GMP-bound Lcd1GAF domain
52.5
Tm of cGMP-bound Lcd1GAF domain
59
Tm of cAMP-bound Lcd1GAF domain
additional information
the addition of cAMP increases the thermal stability of Lcd1GAF_1-180 by 7°C, while cGMP and c-di-GMP do not significantly alter the protein's thermal stability
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
activity decreases with increasing NaCl concentration and in presence of KCl (25 mM)
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
cyclohexane
n-hexane
toluene
cyclohexane
-
at 10% v/v, 97.4% activity remains after 10 min, pH 8.0, 47°C, recombinant enzyme, docking reveals hydrophobic interaction of cyclohexane with amino residues Leu635 and Pro648
cyclohexane
-
at 10% v/v, 97.4% activity remains after 10 min, pH 8.0, 47°C, recombinant enzyme, docking reveals hydrophobic interaction of cyclohexane with amino residues Leu635 and Pro648
-
n-hexane
-
at 10% v/v, 95.3% activity remains after 10 min, pH 8.0, 47°C, recombinant enzyme, docking reveals hydrophobic interaction of nhexane with amino residue Tyr546
n-hexane
-
at 10% v/v, 95.3% activity remains after 10 min, pH 8.0, 47°C, recombinant enzyme, docking reveals hydrophobic interaction of nhexane with amino residue Tyr546
-
toluene
-
at 10% v/v, 95.6% activity remains after 10 min, pH 8.0, 47°C, recombinant enzyme, docking reveals hydrophobic interaction of toluene with amino residues Leu635 and Phe645
toluene
-
at 10% v/v, 95.6% activity remains after 10 min, pH 8.0, 47°C, recombinant enzyme, docking reveals hydrophobic interaction of toluene with amino residues Leu635 and Phe645
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, 25 mM Tris-HCl pH 7.5 including 100 mM NaCl and 1 mM dithiothreitol
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by Ni-NTA affinity chromatography, furthermore a Superdex 200 and a gel filtration column are used
-
from bacterial lysate by metal affinity chromatography and gel-filtration (size-exclusion chromatography), product cyclic di-3,5-guanylate co-purified with wild-type and mutants L170D and L167D from bacterial extracts despite dialysis, nucleotide-free wild-type generated by treatment with phosphodiesterase and subsequent metal affinity chromatography and gel-filtration
-
from bacterial lysate by metal affinity chromatography and gel-filtration, product cyclic di-3,5-guanylate co-purified with wild-type from bacterial extracts despite dialysis, nucleotide-free wild-type generated by treatment with phosphodiesterase and subsequent metal affinity chromatography and gel-filtration
from bacterial lysate by metal affinity chromatography using HisTrap HP column and FPLC (elution: linear imidazole gradient) and dialysis
-
immobilized metal affinity chromatography followed by dialysis and analytical or preparative size exclusion chromatography on Superdex 200 column
metal affinity chromatography (elution with 200 mM imidazole) followed by size-exclusion chromatography on Superdex 200 HR 26/60 column and analytical size-exclusion chromatography on Superdex 200 HR 10/30 column
on a Sephadex G25 and a DEAE-Sepharose column, furthermore an amylose-resin matrix is used
recombinant C-terminally His6-tagged CdgH periplasmic portion
recombinant GST-tagged enzyme from Escherichia coli strain BL21(DE3) by glutathione affinity chromatography, the tag is cleaved off by PreScission protease
-
recombinant His-tagged Lcd1, His-tagged Lcd1GAF domain, and His-tagged Lcd1GAF1-180 domain fragment from Escherichia coli strain BL21(DE3)RP by nickel affinity chromatography and gel filtration
recombinant His6-tagged wild-type enzyme and truncated mutants BpeGReg155, BpeGReg266, and BpeGReg296 from Escherichia coli strain TOP10 by cobalt affinity chromatography
recombinant MBP-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by amylose affinity chromatography, gel filtration, and ultrafiltration
recombinant protein
using a TALON metal affinity resin and a Superdex 200 column
using Ni-NTA chromatography
from bacterial lysate by metal affinity chromatography and gel-filtration, product cyclic di-3,5-guanylate co-purified with wild-type from bacterial extracts despite dialysis, nucleotide-free wild-type generated by treatment with phosphodiesterase and subsequent metal affinity chromatography and gel-filtration
-
from bacterial lysate by metal affinity chromatography and gel-filtration, product cyclic di-3,5-guanylate co-purified with wild-type from bacterial extracts despite dialysis, nucleotide-free wild-type generated by treatment with phosphodiesterase and subsequent metal affinity chromatography and gel-filtration
-
from bacterial lysate by metal affinity chromatography and gel-filtration, product cyclic di-3,5-guanylate co-purified with wild-type from bacterial extracts despite dialysis, nucleotide-free wild-type generated by treatment with phosphodiesterase and subsequent metal affinity chromatography and gel-filtration
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
630-bp internal fragment from bacterial DNA in suicide plasmid pRL277 for construction of suicide plasmid pAM4108 and generation of mutant strains by homologous recombination, complete ORF in pAM2770 for generation of pAM4114 for complementation studies, complete ORF in pEZ-30b(+) (pAM4097) for expression with C-terminal hexa-His-tag in Escherichia coli BL21(DE3)
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a DNA construct encoding the C-terminus of the TM1788 gene is cloned into the vector pET28b+ for expression in Escherichia col BL21DE3 cells
addition of a C-terminal His-tag to GcbC results in a loss of function and stability
cloning and expression of gene LIC13137 (Lcd1), gene fragment LIC13137GAF1-175 (Lcd1GAF), and gene fragment LIC13137GAF1-180 as His-tagged proteins in Escherichia coli strain BL21(DE3)RP
expressed in Escherichia coli as a His-tagged fusion protein
expression as GFP fusion protein for subcellular targeting, expression with His-tag in Escherichia coli
-
expression of MifA or MifB by medium-copy plasmids inhibits motility of Vibrio fischeri. Expression by multicopy plasmids induces further phenotypes correlated with diguanylate cyclase activity such as cellulose biosynthesis and biofilm formation. High-copy expression in Escherichia coli
-
from genomic DNA in pET21 for inducible expression with C-terminal hexa-His-tag in Escherichia coli BL21(DE3)
gene adrA, recombinant overexpression in Pseudomonas fluorescens strain F113 and in Escherichia coli strain DH5alpha
-
gene BP3507, recombinant expression of His6-tagged wild-type enzyme and truncated mutants BpeGReg155, BpeGReg266, and BpeGReg296 in Escherichia coli strain TOP10, recombinant expression of BpeGReg point mutants in Salmonella typhimurium strain ATCC 14028
gene dgcZ, recombinant expression of an DgcZ-mVENUS fusion protein which localizes at one bacterial cell pole in response to alkaline pH and carbon starvation
gene dosC or yddV, stable expression of MBP-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
gene dosC, recombinant expression in Escherichia coli strain TOP10, recombinant expression of EcGReg point mutants in Salmonella typhimurium strain ATCC 14028
gene gcpA, quantitative reverse transcription-PCR enzyme expression analysis
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gene hsbD, phylogenetic analysis, the c-di-GMP synthase gene is encoded in the proximity of the hptB and flagellar genes cluster, recombinant overexpression in Escherichia coli leading to increased intracellular c-di-GMP levels. Recombinant expression of YFP-tagged enzyme, the YFP tag is bound to the DGC domain
gene PA0847, recombinant expression of wild-type and mutant enzymes in PSeusomonas aeruginosa strain PAO1, complementation of PA0847 is applied by amplification of the full-length gene with its native promoter
gene PA3177, quantitative reverse transcription-PCR enzyme expression analysis
in pBR322 for inducible expression with C-terminal hexa-His-tag in Escherichia coli BL21(DE3)pLysS
into an Escherichia coli pUC19-based expression vector and into the vector pMAL-c2e
into the vector pET-33b+ for expression in Escherichia coli BL21DE3 cells
into the vector pET3a for expression in Escherichia coli BL21DE3 cells
overexpressed as an amino-terminal MBP fusion in Escherichia coli
overexpression activates cellulose synthesis in Rhizobium leguminosum and in Agrobacterium tumefaciens
overexpression in Escherichia coli as a His-tagged fusion protein is established and allows production of 2.5 mg of pure c-di-GMP per milligram of YdeH with standard biochemical lab equipment
-
Pseudomonas putida has dozens of DGC/PDE-encoding genes in its genome, identification of the transcription start point of gcsA, cloning of the promoter of gcsA
recombinant expression of GST-tagged enzyme in Escherichia coli strain BL21(DE3)
-
recombinant expression of the C-terminally His6-tagged CdgH periplasmic portion (residues 46-491) including the tandem PBPb-I and PBPb-II domains of the enzyme
recombinant expression of the enzyme in Escherichia coli strain BTH101, recombinant expression of enzyme GcbC wild-type and mutants D413K, E360R, and E429R in Pseudomonas aeruginosa strain UCBPP-PA14, the expression is induced with 0.1% arabinose
recombinantly expressed in Escherichia coli. Target protein is produced mainly in the form of inclusion bodies. Both native and mutant enzymes are not inhibited by the target product during conversion of 1 mM GTP into c-di-GMP
-
residues 142-579 are expressed as a His-tagged fusion protein in Escherichia coli
stably expressed in Escherichia coli as a His-tagged fusion protein
expressed in Escherichia coli as a His-tagged fusion protein
from genomic DNA in pET21 for inducible expression with C-terminal hexa-His-tag in Escherichia coli BL21(DE3)
-
from genomic DNA in pET21 for inducible expression with C-terminal hexa-His-tag in Escherichia coli BL21(DE3)
-
from genomic DNA in pET21 for inducible expression with C-terminal hexa-His-tag in Escherichia coli BL21(DE3)
-
from genomic DNA in pET21 for inducible expression with C-terminal hexa-His-tag in Escherichia coli BL21(DE3)
-
overexpression activates cellulose synthesis in Rhizobium leguminosum and in Agrobacterium tumefaciens
-
overexpression activates cellulose synthesis in Rhizobium leguminosum and in Agrobacterium tumefaciens
-
overexpression activates cellulose synthesis in Rhizobium leguminosum and in Agrobacterium tumefaciens
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
crosstalk between c-di-GMP and cAMP in the regulation of the expression of GcsA in Pseudomonas putida. In terms of transcriptional regulation, gcsA is cooperatively regulated by c-di-GMP and cAMP via their effectors, FleQ and Crp respectively. The transcription of gcsA is inhibited by cAMP. Crp directly regulated the transcription of gcsA by binding to its promoter. cAMP regulates expression of gcsA via Crp, a catabolite activator protein, that binds to the gcsA promoter DNA
crosstalk between c-di-GMP and cAMP in the regulation of the expression of GcsA in Pseudomonas putida. In terms of transcriptional regulation, gcsA is cooperatively regulated by c-di-GMP and cAMP via their effectors, FleQ and Crp respectively. The transcription of gcsA is promoted by c-di-GMP. FleQ indirectly regulated the transcription of gcsA. di-GMP regulates the expression of gcsA via FleQ, an enhancer binding protein of the NtrC family of transcriptional regulators that binds c-di-GMP
FleQ indirectly regulated the transcription of gcsA, while Crp directly regulated the transcription of gcsA by binding to its promoter. c-di-GMP and cAMP cooperatively regulate the expression of gcsA
gene dgcZ transcription is activated by the transcriptional regulator CpxR
transcription of gcsA is cooperatively regulated by c-di-GMP and cAMP via their effectors, FleQ and Crp respectively
crosstalk between c-di-GMP and cAMP in the regulation of the expression of GcsA in Pseudomonas putida. In terms of transcriptional regulation, gcsA is cooperatively regulated by c-di-GMP and cAMP via their effectors, FleQ and Crp respectively. The transcription of gcsA is inhibited by cAMP. Crp directly regulated the transcription of gcsA by binding to its promoter. cAMP regulates expression of gcsA via Crp, a catabolite activator protein, that binds to the gcsA promoter DNA
crosstalk between c-di-GMP and cAMP in the regulation of the expression of GcsA in Pseudomonas putida. In terms of transcriptional regulation, gcsA is cooperatively regulated by c-di-GMP and cAMP via their effectors, FleQ and Crp respectively. The transcription of gcsA is inhibited by cAMP. Crp directly regulated the transcription of gcsA by binding to its promoter. cAMP regulates expression of gcsA via Crp, a catabolite activator protein, that binds to the gcsA promoter DNA
-
-
crosstalk between c-di-GMP and cAMP in the regulation of the expression of GcsA in Pseudomonas putida. In terms of transcriptional regulation, gcsA is cooperatively regulated by c-di-GMP and cAMP via their effectors, FleQ and Crp respectively. The transcription of gcsA is inhibited by cAMP. Crp directly regulated the transcription of gcsA by binding to its promoter. cAMP regulates expression of gcsA via Crp, a catabolite activator protein, that binds to the gcsA promoter DNA
-
-
crosstalk between c-di-GMP and cAMP in the regulation of the expression of GcsA in Pseudomonas putida. In terms of transcriptional regulation, gcsA is cooperatively regulated by c-di-GMP and cAMP via their effectors, FleQ and Crp respectively. The transcription of gcsA is inhibited by cAMP. Crp directly regulated the transcription of gcsA by binding to its promoter. cAMP regulates expression of gcsA via Crp, a catabolite activator protein, that binds to the gcsA promoter DNA
-
-
crosstalk between c-di-GMP and cAMP in the regulation of the expression of GcsA in Pseudomonas putida. In terms of transcriptional regulation, gcsA is cooperatively regulated by c-di-GMP and cAMP via their effectors, FleQ and Crp respectively. The transcription of gcsA is promoted by c-di-GMP. FleQ indirectly regulated the transcription of gcsA. di-GMP regulates the expression of gcsA via FleQ, an enhancer binding protein of the NtrC family of transcriptional regulators that binds c-di-GMP
crosstalk between c-di-GMP and cAMP in the regulation of the expression of GcsA in Pseudomonas putida. In terms of transcriptional regulation, gcsA is cooperatively regulated by c-di-GMP and cAMP via their effectors, FleQ and Crp respectively. The transcription of gcsA is promoted by c-di-GMP. FleQ indirectly regulated the transcription of gcsA. di-GMP regulates the expression of gcsA via FleQ, an enhancer binding protein of the NtrC family of transcriptional regulators that binds c-di-GMP
-
-
crosstalk between c-di-GMP and cAMP in the regulation of the expression of GcsA in Pseudomonas putida. In terms of transcriptional regulation, gcsA is cooperatively regulated by c-di-GMP and cAMP via their effectors, FleQ and Crp respectively. The transcription of gcsA is promoted by c-di-GMP. FleQ indirectly regulated the transcription of gcsA. di-GMP regulates the expression of gcsA via FleQ, an enhancer binding protein of the NtrC family of transcriptional regulators that binds c-di-GMP
-
-
crosstalk between c-di-GMP and cAMP in the regulation of the expression of GcsA in Pseudomonas putida. In terms of transcriptional regulation, gcsA is cooperatively regulated by c-di-GMP and cAMP via their effectors, FleQ and Crp respectively. The transcription of gcsA is promoted by c-di-GMP. FleQ indirectly regulated the transcription of gcsA. di-GMP regulates the expression of gcsA via FleQ, an enhancer binding protein of the NtrC family of transcriptional regulators that binds c-di-GMP
-
-
FleQ indirectly regulated the transcription of gcsA, while Crp directly regulated the transcription of gcsA by binding to its promoter. c-di-GMP and cAMP cooperatively regulate the expression of gcsA
FleQ indirectly regulated the transcription of gcsA, while Crp directly regulated the transcription of gcsA by binding to its promoter. c-di-GMP and cAMP cooperatively regulate the expression of gcsA
-
-
FleQ indirectly regulated the transcription of gcsA, while Crp directly regulated the transcription of gcsA by binding to its promoter. c-di-GMP and cAMP cooperatively regulate the expression of gcsA
-
-
FleQ indirectly regulated the transcription of gcsA, while Crp directly regulated the transcription of gcsA by binding to its promoter. c-di-GMP and cAMP cooperatively regulate the expression of gcsA
-
-
transcription of gcsA is cooperatively regulated by c-di-GMP and cAMP via their effectors, FleQ and Crp respectively
transcription of gcsA is cooperatively regulated by c-di-GMP and cAMP via their effectors, FleQ and Crp respectively
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
-
immobilization of etDGC in sol-gel, a silica matrix that is known to encapsulate biological macromolecules via non-covalent entrapment, is described. The sol-gel matrix preserves the enzymatic activity of the enzyme, and thus, could be a viable method for DGC protein immobilization and c-di-GMP production
medicine
-
diguanylate cyclases are interesting targets for new antimicrobial agents with biofilm activity
molecular biology
-
generation of structural models for product-inhibited, elongated dimer
synthesis
the thermophilic enzyme is a valuable tool for c-di-GMP synthesis as well as the preparation of c-di-GMP derivatives
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ausmees, N.; Mayer, R.; Weinhouse, H.; Volman, G.; Amikam, D.; Benziman, M.; Lindberg, M.
Genetic data indicate that proteins containing the GGDEF domain possess diguanylate cyclase activity
FEMS Microbiol. Lett.
204
163-167
2001
Rhizobium leguminosarum, Escherichia coli, Komagataeibacter xylinus
brenda
Paul, R.; Weiser, S.; Amiot, N.C.; Chan, C.; Schirmer, T.; Giese, B.; Jenal, U.
Cell cycle-dependent dynamic localization of a bacterial response regulator with a novel di-guanylate cyclase output domain
Genes Dev.
18
715-727
2004
Caulobacter vibrioides
brenda
Tal, R.; Wong, H.C.; Calhoon, R.; Gelfand, D.; Fear, A.L.; Volman, G.; Mayer, R.; Ross, P.; Amikam, D.; Weinhouse, H.; Cohen, A.; Sapir, S.; Ohana, P.; Benziman, M.
Three cdg operons control cellular turnover of cyclic di-GMP in Acetobacter xylinum: genetic organization and occurrence of conserved domains in isoenzymes
J. Bacteriol.
180
4416-4425
1998
Komagataeibacter xylinus
brenda
Ryjenkov, D.A.; Tarutina, M.; Moskvin, O.V.; Gomelsky, M.
Cyclic diguanylate is a ubiquitous signaling molecule in bacteria: insights into biochemistry of the GGDEF protein domain
J. Bacteriol.
187
1792-1798
2005
Cereibacter sphaeroides, Borreliella burgdorferi, Cereibacter sphaeroides RSP3513
brenda
O'Shea, T.M.; Klein, A.H.; Geszvain, K.; Wolfe, A.J.; Visick, K.L.
Diguanylate cyclases control magnesium-dependent motility of Vibrio fischeri
J. Bacteriol.
188
8196-8205
2006
Aliivibrio fischeri
brenda
Kuchma, S.L.; Brothers, K.M.; Merritt, J.H.; Liberati, N.T.; Ausubel, F.M.; O'Toole, G.A.
BifA, a cyclic-Di-GMP phosphodiesterase, inversely regulates biofilm formation and swarming motility by Pseudomonas aeruginosa PA14
J. Bacteriol.
189
8165-8178
2007
Pseudomonas aeruginosa
brenda
Christen, B.; Christen, M.; Paul, R.; Schmid, F.; Folcher, M.; Jenoe, P.; Meuwly, M.; Jenal, U.
Allosteric control of cyclic di-GMP signaling
J. Biol. Chem.
281
32015-32024
2006
Caulobacter vibrioides (Q9A3B9)
brenda
Mendez-Ortiz, M.M.; Hyodo, M.; Hayakawa, Y.; Membrillo-Hernandez, J.
Genome-wide transcriptional profile of Escherichia coli in response to high levels of the second messenger 3', 5'-cyclic diguanylic acid. [Erratum to document cited in CA144:426702]
J. Biol. Chem.
282
22248
2007
Escherichia coli
-
brenda
Paul, R.; Abel, S.; Wassmann, P.; Beck, A.; Heerklotz, H.; Jenal, U.
Activation of the diguanylate cyclase PleD by phosphorylation-mediated dimerization
J. Biol. Chem.
282
29170-29177
2007
Caulobacter vibrioides, Caulobacter vibrioides (Q9A5I5)
brenda
Andrade, M.O.; Alegria, M.C.; Guzzo, C.R.; Docena, C.; Rosa, M.C.P.; Ramos, C.H.I.; Farah, C.S.
The HD-GYP domain of RpfG mediates a direct linkage between the Rpf quorum-sensing pathway and a subset of diguanylate cyclase proteins in the phytopathogen Xanthomonas axonopodis pv citri
Mol. Microbiol.
62
537-551
2006
Xanthomonas axonopodis
brenda
Ohana, P.; Delmer, D.P.; Carlson, R.W.; Glushka, J.; Azadi, P.; Bacic, T.; Benziman, M.
Identification of a novel triterpenoid saponin from Pisum sativum as a specific inhibitor of the diguanylate cyclase of Acetobacter xylinum
Plant Cell Physiol.
39
144-152
1998
Komagataeibacter xylinus
brenda
Ohana, P.; Delmer, D.P.; Volman, G.; Benziman, M.
Glycosylated triterpenoid saponin: a specific inhibitor of diguanylate cyclase from Acetobacter xylinum. Biological activity and distribution
Plant Cell Physiol.
39
153-159
1998
Komagataeibacter xylinus
-
brenda
Chan, C.; Paul, R.; Samoray, D.; Amiot, N.C.; Giese, B.; Jenal, U.; Schirmer, T.
Structural basis of activity and allosteric control of diguanylate cyclase
Proc. Natl. Acad. Sci. USA
101
17084-17089
2004
Caulobacter vibrioides
brenda
Wassmann, P.; Chan, C.; Paul, R.; Beck, A.; Heerklotz, H.; Jenal, U.; Schirmer, T.
Structure of BeF3--modified response regulator PleD: implications for diguanylate cyclase activation, catalysis, and feedback inhibition
Structure
15
915-927
2007
Caulobacter vibrioides, Caulobacter vibrioides (Q9A5I5)
brenda
Neunuebel, M.R.; Golden, J.W.
The Anabaena sp. strain PCC 7120 gene all2874 encodes a diguanylate cyclase and is required for normal heterocyst development under high-light growth conditions
J. Bacteriol.
190
6829-6836
2008
Anabaena sp.
brenda
De, N.; Pirruccello, M.; Krasteva, P.V.; Bae, N.; Raghavan, R.V.; Sondermann, H.
Phosphorylation-independent regulation of the diguanylate cyclase WspR
PLoS Biol.
6
601-617
2008
Pseudomonas aeruginosa, Pseudomonas fluorescens, Pseudomonas fluorescens PfO-1, Pseudomonas putida, Pseudomonas putida KT 2240, Pseudomonas syringae, Pseudomonas syringae DC3000
brenda
Rao, F.; Pasunooti, S.; Ng, Y.; Zhuo, W.; Lim, L.; Liu, A.W.; Liang, Z.X.
Enzymatic synthesis of c-di-GMP using a thermophilic diguanylate cyclase
Anal. Biochem.
389
138-142
2009
Thermotoga maritima (Q9X2A8)
brenda
Antoniani, D.; Bocci, P.; Maciag, A.; Raffaelli, N.; Landini, P.
Monitoring of diguanylate cyclase activity and of cyclic-di-GMP biosynthesis by whole-cell assays suitable for high-throughput screening of biofilm inhibitors
Appl. Microbiol. Biotechnol.
85
1095-1104
2010
Escherichia coli
brenda
Tuckerman, J.R.; Gonzalez, G.; Sousa, E.H.; Wan, X.; Saito, J.A.; Alam, M.; Gilles-Gonzalez, M.A.
An oxygen-sensing diguanylate cyclase and phosphodiesterase couple for c-di-GMP control
Biochemistry
48
9764-9774
2009
Escherichia coli (P0AA89), Escherichia coli
brenda
Sawai, H.; Yoshioka, S.; Uchida, T.; Hyodo, M.; Hayakawa, Y.; Ishimori, K.; Aono, S.
Molecular oxygen regulates the enzymatic activity of a heme-containing diguanylate cyclase (HemDGC) for the synthesis of cyclic di-GMP
Biochim. Biophys. Acta
1804
166-172
2010
Desulfotalea psychrophila (Q6ARU5), Desulfotalea psychrophila
brenda
Lai, T.H.; Kumagai, Y.; Hyodo, M.; Hayakawa, Y.; Rikihisa, Y.
The Anaplasma phagocytophilum PleC histidine kinase and PleD diguanylate cyclase two-component system and role of cyclic Di-GMP in host cell infection
J. Bacteriol.
191
693-700
2009
Anaplasma phagocytophilum (Q2GKF8), Anaplasma phagocytophilum
brenda
De, N.; Navarro, M.V.; Raghavan, R.V.; Sondermann, H.
Determinants for the activation and autoinhibition of the diguanylate cyclase response regulator WspR
J. Mol. Biol.
393
619-633
2009
Pseudomonas syringae
brenda
Sambanthamoorthy, K.; Sloup, R.E.; Parashar, V.; Smith, J.M.; Kim, E.E.; Semmelhack, M.F.; Neiditch, M.B.; Waters, C.M.
Identification of small molecules that antagonize diguanylate cyclase enzymes to inhibit biofilm formation
Antimicrob. Agents Chemother.
56
5202-5211
2012
Pseudomonas aeruginosa, Vibrio cholerae (Q9KPJ7), Vibrio cholerae
brenda
Zaehringer, F.; Massa, C.; Schirmer, T.
Efficient enzymatic production of the bacterial second messenger c-di-GMP by the diguanylate cyclase YdeH from E. coli
Appl. Biochem. Biotechnol.
163
71-79
2011
Escherichia coli
brenda
Tran, N.T.; Den Hengst, C.D.; Gomez-Escribano, J.P.; Buttner, M.J.
Identification and characterization of CdgB, a diguanylate cyclase involved in developmental processes in Streptomyces coelicolor
J. Bacteriol.
193
3100-3108
2011
Streptomyces coelicolor
brenda
Newell, P.; Yoshioka, S.; Hvorecny, K.; Monds, R.; OToole, G.
Systematic analysis of diguanylate cyclases that promote biofilm formation by Pseudomonas fluorescens Pf0-1
J. Bacteriol.
193
4685-4698
2011
Pseudomonas fluorescens, Pseudomonas fluorescens (Q3KFC4), Pseudomonas fluorescens (Q3K751)
brenda
Korovashkina, A.; Rymko, A.; Kvach, S.; Zinchenko, A.
Enzymatic synthesis of c-di-GMP using inclusion bodies of Thermotoga maritima full-length diguanylate cyclase
J. Biotechnol.
164
276-280
2013
Thermotoga maritima
brenda
Pasunooti, S.; Surya, W.; Tan, S.; Liang, Z.
Sol-gel immobilization of a thermophilic diguanylate cyclase for enzymatic production of cyclic-di-GMP
J. Mol. Catal. B
67
98-103
2010
Thermotoga maritima
-
brenda
Spangler, C.; Kaever, V.; Seifert, R.
Interaction of the diguanylate cyclase YdeH of Escherichia coli with 2,(3)-substituted purine and pyrimidine nucleotides
J. Pharmacol. Exp. Ther.
336
234-241
2011
Escherichia coli
brenda
Vorobiev, S.M.; Neely, H.; Yu, B.; Seetharaman, J.; Xiao, R.; Acton, T.B.; Montelione, G.T.; Hunt, J.F.
Crystal structure of a catalytically active GG(D/E)EF diguanylate cyclase domain from Marinobacter aquaeolei with bound c-di-GMP product
J. Struct. Funct. Genomics
13
177-183
2012
Marinobacter nauticus (A1U3W3)
brenda
Merritt, J.; Ha, D.; Cowles, K.; Lu, W.; Morales, D.; Rabinowitz, J.; Gitai, Z.; O'Toole, G.
Specific control of Pseudomonas aeruginosa surface-associated behaviors by two c-di-GMP diguanylate cyclases
mBio
1
e00183
2010
Pseudomonas aeruginosa (Q9I4M8), Pseudomonas aeruginosa (Q9HW69), Pseudomonas aeruginosa
brenda
Tagliabue, L.; Antoniani, D.; Maciag, A.; Bocci, P.; Raffaelli, N.; Landini, P.
The diguanylate cyclase YddV controls production of the exopolysaccharide poly-N-acetylglucosamine (PNAG) through regulation of the PNAG biosynthetic pgaABCD operon
Microbiology
156
2901-2911
2010
Escherichia coli
brenda
Liu, N.; Pak, T.; Boon, E.M.
Characterization of a diguanylate cyclase from Shewanella woodyi with cyclase and phosphodiesterase activities
Mol. Biosyst.
6
1561-1564
2010
Shewanella woodyi
brenda
Kostick, J.L.; Szkotnicki, L.T.; Rogers, E.A.; Bocci, P.; Raffaelli, N.; Marconi, R.T.
The diguanylate cyclase, Rrp1, regulates critical steps in the enzootic cycle of the Lyme disease spirochetes
Mol. Microbiol.
81
219-231
2011
Borreliella burgdorferi
brenda
Tarnawski, M.; Barends, T.R.; Schlichting, I.
Structural analysis of an oxygen-regulated diguanylate cyclase
Acta Crystallogr. Sect. D
71
2158-2177
2015
Escherichia coli (P0AA89), Escherichia coli
brenda
Hunter, J.; Severin, G.; Koestler, B.; Waters, C.
The Vibrio cholerae diguanylate cyclase VCA0965 has an AGDEF active site and synthesizes cyclic di-GMP
BMC Microbiol.
14
22
2014
Vibrio cholerae serotype O1, Vibrio cholerae serotype O1 C6706str2
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brenda
Aragon, I.M.; Perez-Mendoza, D.; Moscoso, J.A.; Faure, E.; Guery, B.; Gallegos, M.T.; Filloux, A.; Ramos, C.
Diguanylate cyclase DgcP is involved in plant and human Pseudomonas spp. infections
Environ. Microbiol.
17
4332-4351
2015
Pseudomonas aeruginosa (S0JAX7), Pseudomonas aeruginosa, Pseudomonas savastanoi pv. savastanoi, Pseudomonas aeruginosa PAK (S0JAX7), Pseudomonas savastanoi pv. savastanoi NCPPB 3335
brenda
Chaudhuri, S.; Pratap, S.; Paromov, V.; Li, Z.; Mantri, C.K.; Xie, H.
Identification of a diguanylate cyclase and its role in Porphyromonas gingivalis virulence
Infect. Immun.
82
2728-2735
2014
Porphyromonas gingivalis (B2RM56), Porphyromonas gingivalis, Porphyromonas gingivalis DSM 20709 (B2RM56)
brenda
Barnhart, D.M.; Su, S.; Farrand, S.K.
A signaling pathway involving the diguanylate cyclase CelR and the response regulator DivK controls cellulose synthesis in Agrobacterium tumefaciens
J. Bacteriol.
196
1257-1274
2014
Agrobacterium tumefaciens
brenda
Petrova, O.E.; Cherny, K.E.; Sauer, K.
The Pseudomonas aeruginosa diguanylate cyclase GcbA, a homolog of P. fluorescens GcbA, promotes initial attachment to surfaces, but not biofilm formation, via regulation of motility
J. Bacteriol.
196
2827-2841
2014
Pseudomonas aeruginosa, Pseudomonas fluorescens
brenda
Enomoto, G.; Nomura, R.; Shimada, T.; Ni-Ni-Win, T.; Narikawa, R.; Ikeuchi, M.
Cyanobacteriochrome SesA is a diguanylate cyclase that induces cell aggregation in Thermosynechococcus
J. Biol. Chem.
289
24801-24809
2014
Thermosynechococcus vestitus (Q8DKD5)
brenda
Oliveira, M.C.; Teixeira, R.D.; Andrade, M.O.; Pinheiro, G.M.; Ramos, C.H.; Farah, C.S.
Cooperative substrate binding by a diguanylate cyclase
J. Mol. Biol.
427
415-432
2015
Xanthomonas citri pv. citri (Q8PPS5), Xanthomonas citri pv. citri
brenda
Huangyutitham, V.; Guevener, Z.T.; Harwood, C.S.
Subcellular clustering of the phosphorylated WspR response regulator protein stimulates its diguanylate cyclase activity
MBio
4
e00242
2013
Pseudomonas aeruginosa (Q9HXT9), Pseudomonas aeruginosa
brenda
Engl, C.; Waite, C.J.; McKenna, J.F.; Bennett, M.H.; Hamann, T.; Buck, M.
Chp8, a diguanylate cyclase from Pseudomonas syringae pv. Tomato DC3000, suppresses the pathogen-associated molecular pattern flagellin, increases extracellular polysaccharides, and promotes plant immune evasion
MBio
5
e01168
2014
Pseudomonas syringae pv. tomato, Pseudomonas syringae pv. tomato DC3000
brenda
Dahlstrom, K.M.; Giglio, K.M.; Collins, A.J.; Sondermann, H.; OToole, G.A.
Contribution of physical interactions to signaling specificity between a diguanylate cyclase and its effector
MBio
6
e01978-15
2015
Pseudomonas fluorescens (Q3K751), Pseudomonas fluorescens, Pseudomonas fluorescens Pf0-1 (Q3K751)
brenda
Kim, H.; Harshey, R.
A diguanylate cyclase acts as a cell division inhibitor in a two-step response to reductive and envelope stresses
MBio
7
e00822
2016
Escherichia coli (P46139)
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brenda
Rotcheewaphan, S.; Belisle, J.T.; Webb, K.J.; Kim, H.J.; Spencer, J.S.; Borlee, B.R.
Diguanylate cyclase activity of the Mycobacterium leprae T cell antigen ML1419c
Microbiology
162
1651-1661
2016
Mycobacterium leprae (Q7AQ57), Mycobacterium leprae, Mycobacterium leprae TN (Q7AQ57)
brenda
Deepthi, A.; Liew, C.W.; Liang, Z.X.; Swaminathan, K.; Lescar, J.
Structure of a diguanylate cyclase from Thermotoga maritima: insights into activation, feedback inhibition and thermostability
PLoS ONE
9
e110912
2014
Thermotoga maritima (Q9X2A8), Thermotoga maritima, Thermotoga maritima DSM 3109 (Q9X2A8)
brenda
Ramirez-Mata, A.; Lopez-Lara, L.I.; Xiqui-Vazquez, M.L.; Jijon-Moreno, S.; Romero-Osorio, A.; Baca, B.E.
The cyclic-di-GMP diguanylate cyclase CdgA has a role in biofilm formation and exopolysaccharide production in Azospirillum brasilense
Res. Microbiol.
167
190-201
2016
Azospirillum brasilense (A0A0Y0RFK5), Azospirillum brasilense, Azospirillum brasilense Sp7 (A0A0Y0RFK5), Azospirillum brasilense Sp7
brenda
Wu, C.; Cheng, Y.Y.; Yin, H.; Song, X.N.; Li, W.W.; Zhou, X.X.; Zhao, L.P.; Tian, L.J.; Han, J.C.; Yu, H.Q.
Oxygen promotes biofilm formation of Shewanella putrefaciens CN32 through a diguanylate cyclase and an adhesin
Sci. Rep.
3
1945
2013
Shewanella putrefaciens, Shewanella putrefaciens CN32
brenda
Su, J.; Zou, X.; Huang, L.; Bai, T.; Liu, S.; Yuan, M.; Chou, S.H.; He, Y.W.; Wang, H.; He, J.
DgcA, a diguanylate cyclase from Xanthomonas oryzae pv. oryzae regulates bacterial pathogenicity on rice
Sci. Rep.
6
25978
2016
Xanthomonas oryzae pv. oryzae (Q5GVN1), Xanthomonas oryzae pv. oryzae, Xanthomonas oryzae pv. oryzae KXO85 (Q5GVN1)
brenda
Chen, Y.; Liu, S.; Liu, C.; Huang, Y.; Chi, K.; Su, T.; Zhu, D.; Peng, J.; Xia, Z.; He, J.; Xu, S.; Hu, W.; Gu, L.
Dcsbis (PA2771) from Pseudomonas aeruginosa is a highly active diguanylate cyclase with unique activity regulation
Sci. Rep.
6
29499
2016
Pseudomonas aeruginosa (Q9I072), Pseudomonas aeruginosa, Pseudomonas aeruginosa DSM 22644 (Q9I072)
brenda
Zaehringer, F.; Lacanna, E.; Jenal, U.; Schirmer, T.; Boehm, A.
Structure and signaling mechanism of a zinc-sensory diguanylate cyclase
Structure
21
1149-1157
2013
Escherichia coli (P31129), Escherichia coli
brenda
Dahlstrom, K.M.; O'Toole, G.A.
A symphony of cyclases specificity in diguanylate cyclase signaling
Annu. Rev. Microbiol.
71
179-195
2017
Komagataeibacter xylinus (O87374), Escherichia coli (P0AA89), Caulobacter vibrioides, Pseudomonas aeruginosa, Vibrio cholerae serotype O1, Burkholderia cenocepacia, Clostridioides difficile, Vibrio cholerae serotype O1 A1552
brenda
Poudyal, B.; Sauer, K.
The PA3177 gene encodes an active diguanylate cyclase that contributes to biofilm antimicrobial tolerance but not biofilm formation by Pseudomonas aeruginosa
Antimicrob. Agents Chemother.
62
e01049-18
2018
Pseudomonas aeruginosa (Q9HZ57), Pseudomonas aeruginosa, Pseudomonas aeruginosa ATCC 15692 (Q9HZ57), Pseudomonas aeruginosa DSM 22644 (Q9HZ57), Pseudomonas aeruginosa CIP 104116 (Q9HZ57), Pseudomonas aeruginosa JCM 14847 (Q9HZ57), Pseudomonas aeruginosa LMG 12228 (Q9HZ57), Pseudomonas aeruginosa 1C (Q9HZ57), Pseudomonas aeruginosa PRS 101 (Q9HZ57)
brenda
Zhu, B.; Liu, C.; Liu, S.; Cong, H.; Chen, Y.; Gu, L.; Ma, L.Z.
Membrane association of SadC enhances its diguanylate cyclase activity to control exopolysaccharides synthesis and biofilm formation in Pseudomonas aeruginosa
Environ. Microbiol.
18
3440-3452
2016
Pseudomonas aeruginosa (Q9HW69), Pseudomonas aeruginosa, Pseudomonas aeruginosa ATCC 15692 (Q9HW69), Pseudomonas aeruginosa DSM 22644 (Q9HW69), Pseudomonas aeruginosa CIP 104116 (Q9HW69), Pseudomonas aeruginosa JCM 14847 (Q9HW69), Pseudomonas aeruginosa LMG 12228 (Q9HW69), Pseudomonas aeruginosa 1C (Q9HW69), Pseudomonas aeruginosa PRS 101 (Q9HW69)
brenda
Xiao, Y.; Liu, H.; He, M.; Nie, L.; Nie, H.; Chen, W.; Huang, Q.
A crosstalk between c-di-GMP and cAMP in regulating transcription of GcsA, a diguanylate cyclase involved in swimming motility in Pseudomonas putida
Environ. Microbiol.
22
142-157
2020
Pseudomonas putida, Pseudomonas putida (Q88GL0), Pseudomonas putida ATCC 47054 (Q88GL0), Pseudomonas putida DSM 6125 (Q88GL0), Pseudomonas putida DSM 6125, Pseudomonas putida NCIMB 11950 (Q88GL0)
brenda
Biswas, S.; Chouhan, O.; Bandekar, D.
Diguanylate cyclases in Vibrio cholerae essential regulators of lifestyle switching
Front. Cell. Infect. Microbiol.
10
582947
2020
Vibrio cholerae, Vibrio cholerae serotype O1 (Q9KKY5), Vibrio cholerae serotype O1 (A0A0H3AFM6), Vibrio cholerae serotype O1 ATCC 39315 (Q9KKY5), Vibrio cholerae serotype O1 ATCC 39541 (A0A0H3AFM6), Vibrio cholerae serotype O1 Classical Ogawa 395 (A0A0H3AFM6), Vibrio cholerae serotype O1 El Tor Inaba N16961 (Q9KKY5), Vibrio cholerae serotype O1 O395 (A0A0H3AFM6)
brenda
Cho, K.H.; Tryon, R.G.; Kim, J.H.
Screening for diguanylate cyclase (DGC) inhibitors mitigating bacterial biofilm formation
Front. Chem.
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264
2020
Caulobacter vibrioides (A0A0H3CCZ8), Caulobacter vibrioides (B8GZM2), Pseudomonas aeruginosa (Q9HXT9), Pseudomonas aeruginosa (Q9HT84), Clostridioides difficile (A0A170Y3L9), Salmonella enterica subsp. enterica serovar Typhimurium (Q8ZNT5), Vibrio cholerae serotype O1 (Q9KKZ4), Komagataeibacter xylinus (O87374), Synechocystis sp. PCC 6803 (P73272), Caulobacter vibrioides NA1000 (A0A0H3CCZ8), Caulobacter vibrioides NA1000 (B8GZM2), Pseudomonas aeruginosa ATCC 15692 (Q9HT84), Pseudomonas aeruginosa ATCC 15692 (Q9HXT9), Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720 (Q8ZNT5), Pseudomonas aeruginosa DSM 22644 (Q9HT84), Pseudomonas aeruginosa DSM 22644 (Q9HXT9), Vibrio cholerae serotype O1 ATCC 39315 (Q9KKZ4), Vibrio cholerae serotype O1 El Tor Inaba N16961 (Q9KKZ4), Pseudomonas aeruginosa CIP 104116 (Q9HT84), Pseudomonas aeruginosa CIP 104116 (Q9HXT9), Pseudomonas aeruginosa JCM 14847 (Q9HT84), Pseudomonas aeruginosa JCM 14847 (Q9HXT9), Pseudomonas aeruginosa LMG 12228 (Q9HT84), Pseudomonas aeruginosa LMG 12228 (Q9HXT9), Pseudomonas aeruginosa 1C (Q9HT84), Pseudomonas aeruginosa 1C (Q9HXT9), Pseudomonas aeruginosa PRS 101 (Q9HT84), Pseudomonas aeruginosa PRS 101 (Q9HXT9), Salmonella enterica subsp. enterica serovar Typhimurium SGSC1412 (Q8ZNT5), Caulobacter vibrioides CB15N (A0A0H3CCZ8)
brenda
Zhang, Y.; Guo, J.; Zhang, N.; Yuan, W.; Lin, Z.; Huang, W.
Characterization and analysis of a novel diguanylate cyclase PA0847 from Pseudomonas aeruginosa PAO1
Infect. Drug Resist.
12
655-665
2019
Pseudomonas aeruginosa (Q9I594), Pseudomonas aeruginosa ATCC 15692 (Q9I594), Pseudomonas aeruginosa DSM 22644 (Q9I594), Pseudomonas aeruginosa CIP 104116 (Q9I594), Pseudomonas aeruginosa JCM 14847 (Q9I594), Pseudomonas aeruginosa LMG 12228 (Q9I594), Pseudomonas aeruginosa 1C (Q9I594), Pseudomonas aeruginosa PRS 101 (Q9I594)
brenda
Fernicola, S.; Paiardini, A.; Giardina, G.; Rampioni, G.; Leoni, L.; Cutruzzolxa0, F.; Rinaldo, S.
In silico discovery and in vitro validation of catechol-containing sulfonohydrazide compounds as potent inhibitors of the diguanylate cyclase PleD
J. Bacteriol.
198
147-156
2016
Caulobacter vibrioides (Q9A5I5), Caulobacter vibrioides, Pseudomonas aeruginosa (Q9HXT9), Pseudomonas aeruginosa (A0A0C7ADU5), Caulobacter vibrioides CB15 (Q9A5I5), Pseudomonas aeruginosa ATCC 15692 (Q9HXT9), Pseudomonas aeruginosa DSM 22644 (Q9HXT9), Caulobacter vibrioides ATCC 19089 (Q9A5I5), Pseudomonas aeruginosa CIP 104116 (Q9HXT9), Pseudomonas aeruginosa JCM 14847 (Q9HXT9), Pseudomonas aeruginosa LMG 12228 (Q9HXT9), Pseudomonas aeruginosa 1C (Q9HXT9), Pseudomonas aeruginosa PRS 101 (Q9HXT9)
brenda
Dahlstrom, K.M.; Giglio, K.M.; Sondermann, H.; OToole, G.A.
The inhibitory site of a diguanylate cyclase is a necessary element for interaction and signaling with an effector protein
J. Bacteriol.
198
1595-1603
2016
Pseudomonas fluorescens (Q3K751), Pseudomonas fluorescens, Pseudomonas fluorescens Pfl01 (Q3K751)
brenda
Lacanna, E.; Bigosch, C.; Kaever, V.; Boehm, A.; Becker, A.
Evidence for Escherichia coli diguanylate cyclase DgcZ interlinking surface sensing and adhesion via multiple regulatory routes
J. Bacteriol.
198
2524-2535
2016
Escherichia coli (P31129), Escherichia coli
brenda
Lengalova, A.; Fojtikova-Proskova, V.; Vavra, J.; Martinek, V.; Stranava, M.; Shimizu, T.; Martinkova, M.
Kinetic analysis of a globin-coupled diguanylate cyclase, YddV effects of heme iron redox state, axial ligands, and heme distal mutations on catalysis
J. Inorg. Biochem.
201
110833
2019
Escherichia coli (P0AA89), Escherichia coli
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da Costa Vasconcelos, F.N.; Maciel, N.K.; Favaro, D.C.; de Oliveira, L.C.; Barbosa, A.S.; Salinas, R.K.; de Souza, R.F.; Farah, C.S.; Guzzo, C.R.
Structural and enzymatic characterization of a cAMP-dependent diguanylate cyclase from pathogenic Leptospira species
J. Mol. Biol.
429
2337-2352
2017
Leptospira interrogans serovar Copenhageni str. Fiocruz L1-130 (Q72MQ6)
brenda
Angerer, V.; Schwenk, P.; Wallner, T.; Kaever, V.; Hiltbrunner, A.; Wilde, A.
The protein Slr1143 is an active diguanylate cyclase in Synechocystis sp. PCC 6803 and interacts with the photoreceptor Cph2
Microbiology
163
920-930
2017
Synechocystis sp. PCC 6803 (P73272)
brenda
Yuan, X.; Tian, F.; He, C.; Severin, G.B.; Waters, C.M.; Zeng, Q.; Liu, F.; Yang, C.H.
The diguanylate cyclase GcpA inhibits the production of pectate lyases via the H-NS protein and RsmB regulatory RNA in Dickeya dadantii
Mol. Plant Pathol.
19
1873-1886
2018
Dickeya dadantii, Dickeya dadantii 3937
brenda
Valentini, M.; Laventie, B.J.; Moscoso, J.; Jenal, U.; Filloux, A.
The diguanylate cyclase HsbD intersects with the HptB regulatory cascade to control Pseudomonas aeruginosa biofilm and motility
PLoS Genet.
12
e1006354
2016
Pseudomonas aeruginosa (Q9HYQ2), Pseudomonas aeruginosa, Pseudomonas aeruginosa ATCC 15692 (Q9HYQ2)
brenda
Wan, X.; Saito, J.; Newhouse, J.; Hou, S.; Alam, M.
The importance of conserved amino acids in heme-based globin-coupled diguanylate cyclases
PLoS ONE
12
e0182782
2017
Bordetella pertussis (Q7VTL8), Bordetella pertussis, Bordetella pertussis ATCC BAA-589 (Q7VTL8), Bordetella pertussis NCTC 13251 (Q7VTL8), Bordetella pertussis Tohama I (Q7VTL8), Escherichia coli (P0AA89), Escherichia coli
brenda
Kuang, S.; Yuan, Y.; Wu, Z.; Peng, R.
Expression, purification and characterization of diguanylate cyclase from Rhodococcus ruber
Protein Expr. Purif.
163
105441
2019
Rhodococcus ruber, Rhodococcus ruber SD3
brenda
Xu, M.; Wang, Y.Z.; Yang, X.A.; Jiang, T.; Xie, W.
Structural studies of the periplasmic portion of the diguanylate cyclase CdgH from Vibrio cholerae
Sci. Rep.
7
1861
2017
Vibrio cholerae serotype O1 (Q9KT38), Vibrio cholerae serotype O1 ATCC 39315 (Q9KT38), Vibrio cholerae serotype O1 El Tor Inaba N16961 (Q9KT38)
brenda
Muriel, C.; Blanco-Romero, E.; Trampari, E.; Arrebola, E.; Duran, D.; Redondo-Nieto, M.; Malone, J.G.; Martin, M.; Rivilla, R.
The diguanylate cyclase AdrA regulates flagellar biosynthesis in Pseudomonas fluorescens F113 through SadB
Sci. Rep.
9
8096
2019
Pseudomonas fluorescens, Pseudomonas fluorescens F113
brenda
EXTERNAL LINKS (specific for EC-Number 2.7.7.65)
Transporter Classification Database (TCDB): 9.B.34.1.4, 9.B.34.1.2
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Release 2026.1 (March 2026)
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